Prof. Dr. Scheibel, Thomas

Open Resume

Proteinassemblierung/Verarbeitung

Die Forschungsgruppe „Protein Assembly and Processing“ beschäftigt sich mit der Erforschung und Entwicklung verschiedener Verarbeitungsmethoden von Proteinmaterialien und deren Anwendungen. Unterschiedliche Proteine, darunter rekombinante Spinnenseide, werden zu Filmen, Schäumen, Hydrogelen, (Nano-)Fibrillen, Beschichtungen und Hybridmaterialien verarbeitet. Die daraus resultierende Wirkung und mögliche Anwendungen werden im Hinblick auf bakterielle Abstoßung, bakteriostatische Eigenschaften, zellspezifische Interaktion und mechanische Eigenschaften analysiert.

Research Projects

Heinritz, Christina (M. Sc.)

christina1.heinritz(.at.)uni-bayreuth.de

0921 55-6708

Entwicklung und Produktion bioinspirierter Kleber

Synthetische Klebstoffe verbinden Gegenstände miteinander. In der Natur vorkommende adhäsive Systeme dagegen sind multifunktional und werden für verschiede Vorgänge wie z.B. zum Schutz, zur Selbstverteidigung und Fortpflanzung, sowie zum Jagen und Fangen von Beute verwendet. Bei natürlichen „Klebern“ handelt es sich oftmals um Proteine, die typische Aminosäuren oder Motive in Verbindung mit post-translationalen Modifikationen enthalten. Ein gut untersuchtes Beispiel im Bereich der Unterwasser-Adhäsive sind die Muschelfußproteine (mfp) der Miesmuschel (Mytilus edulis), die sich auf unterschiedlichen Oberflächen im Meer verankern können. Es ist bekannt, dass hohe Lysin- und DOPA- (3, 4-Dihydroxyphenylalanin) Konzentrationen die entscheidenden Faktoren für die Klebeverbindungen sind. Darüber hinaus nutzen andere Lebewesen Serin- und Threonin-reiche Motive, welche zum Teil durch Phosphorylierungen oder Glycosylierungen modifiziert sind.

Einige protein-basierte Klebesysteme sollen genauer charakterisiert werden. Das Verständnis der Adhäsionsmechanismen erlaubt dann deren Nachahmung und die Entwicklung anwendungsspezifischer rekombinant hergestellter Klebeproteine.

Mohotti, Supun

supun.mohotti(.at.)uni-bayreuth.de

0921 55-6718

Chemische Modifikation von Spinnenseide

Hybridmaterialien auf Proteinbasis

Protein-Polymer-Hybridmaterialien sind aufgrund ihrer einstellbaren Eigenschaften für viele Anwendungen interessant. Polymere können so gestaltet werden, dass sie verschiedene Architekturen, Kettenlängen, Verzweigungen, Seitenkettenfunktionalitäten und Reizempfindlichkeiten aufweisen. Infolgedessen ermöglichen Protein-Polymer-Hybride die Herstellung von Hybridmaterialien, mit denen gängige physikalische Beschränkungen (Temperatur, pH-Wert und Abbau) überwunden werden können, während die Zielspezifität und Bioaktivität der Proteine erhalten bleibt. Durch kovalente Kopplung thiolhaltiger Protein-Domänen an bifunktionelle Prä-Polymere sollen trigger-empfindliche Polymersysteme erzeugt werden. Sobald solche Protein-Polymer-Konjugate etabliert sind, könnten sie für kontrollierte Assemblierungs- Dissemblieungszyklen von Hydrogelen unter pH- und Salzkontrolle verwendet werden, was Anwendungen z.B. in Wirkstoff-Transportsysteme und in der Biofabrikation ermöglicht.

P2: Methacrylierung von Spinnenseide zur Herstellung von photo-empfindlichen Biotinten

Um chemische Vernetzungen und stimuli-responsive Materialien mit einstellbaren Eigenschaften zu erhalten, ist eine chemische Modifizierung rekombinanter Spinnenseide erforderlich. Die Methacrylierung ist eine vielversprechende Methode, um die oben genannten Eigenschaften zu erreichen, da sie der Spinnenseide eine Methacrylfunktionalität verleiht. Der Schwerpunkt liegt auf der Einführung von UV-Vernetzungstrigger in Spinnenseide und der anschließenden Entwicklung neuer vernetzter polymerer Materialien.

Publications

Troßmann, V. & Scheibel, T.

Spider silk and blend biomaterials: recent advances and future opportunities

Silk-Based Biomaterials for Tissue Engineering, Regenerative and Precision Medicine. Woodhead Publishing Series in Biomaterials 2024, Pages 133-190

Charlotte Hopfe, Bryan Ospina-Jara, Thilo Schulze, Marta Tischer, Diego Morales, Vivien Reinhartz, Rashin Esghi Esfahani, Carlos Valderrama, José-Pérez-Rigueiro, Christoph Bleidorn, Heike Feldhaar, Jimmy Cabra-Garcia & Thomas Scheibel

Impact of environmental factors on spider silk properties

Lang, G., Grill, C. & Scheibel, T.

Site-specific functionalization of recombinant spider silk Janus fibers

Shakir Zainuddin & Thomas Scheibel

Continuous yarn electrospinning

Matthias Völkl, Valérie Jérome, Alfons Weig, Julia Jasinski, Nora Meides, Peter Strohriegl, Thomas Scheibel & Ruth Freitag

Pristine and artificially-aged polystyrene microplastic particles differ in regard to cellular response

Sawan Shetty, Selvakumar Murugesan, Sahar Salehi, Alexandra Pellert, Melanie Scheibel, Thomas Scheibel & Srinivasan Anandhan

Evaluation of piezoelectric behavior and biocompatibility of poly(vinylidene fluoride) ultrafine fibers with incorporated talc nanosheets

Nicholas J. Chan, Sarah Lentz, Paul A. Gurr, Thomas Scheibel & Greg G. Qiao

Mimicry of silk utilizing synthetic polypeptides

Sarah Lentz, Vanessa T. Troßmann, Christian B. Borkner, Vivien Beyersdorfer, Mrkus Rottmar & Thomas Scheibel

Structure−Property Relationship Based on the Amino Acid Composition of Recombinant Spider Silk Proteins for Potential Biomedical Applications

Vanessa T. Troßmann, Stefanie Heltmann-Meyer, Hanna Amouei, Harald Wajantm, Raymund E. Horch, Dominik Steiner & Thomas Scheibel

Recombinant Spider Silk Bioinks for Continuous Protein Release by Encapsulated Producer Cells

Hendrik Bargel, Vanessa Troßmann, Christoph Sommer & Thomas Scheibel

Bioselectivity of silk protein-based materials and their bio-inspired applications

Vanessa J. Neubauer, Florian Hüter, Johannes Wittmann, Vanessa T. Troßmann, Claudia Kleinschrodt, Bettina Alber-Laukant, Frank Rieg & Thomas Scheibel

Flow Simulation and Gradient Printing of Fluorapatite- and Cell-Loaded Recombinant Spider Silk Hydrogels

Julia Jasinski, Magdalena V. Wilde, Matthias Voelkl, Valérie Jerôme, Thomas Fröhlich, Ruth Freitag und Thomas Scheibel

Tailor-Made Protein Corona Formation on Polystyrene Microparticles and its Effect on Epithelial Cell Uptake

Sarah Lentz, Vanessa T. Troßmann & Thomas Scheibel

Selective Topography Directed Cell Adhesion on Spider Silk Surfaces

Mirjam Hofmaier, Mikhail Malanin, Eva Bittrich, Sarah Lentz, Birgit Urban, Thomas Scheibel, Andreas Fery & Martin Müller

β‑Sheet structure formation within binary blends of two spider silk related peptides

Vanessa T. Trossmann & Thomas Scheibel

Design of Recombinant Spider Silk Proteins for Cell Type Specific Binding

Martin Reimer, Kai Mayer, Daniel Van Opdenbosch, Thomas Scheibel, & Cordt Zollfrank

Biocompatible Optical Fibers Made of Regenerated Cellulose and Recombinant Cellulose-Binding Spider Silk

Lamberger, Z., Zainuddin, S., Scheibel, T. & Lang, G.

Polymeric Janus Fibers

Saric, M. & Scheibel, T.

Two-in-One Spider Silk Protein with Combined Mechanical Features in All-Aqueous Spun Fibers

D. Stengel, M. Saric, H. R. Johnson, T. Schiller, J. Diehl, K. Chalek, D. Onofrei, T. Scheibel, G. H. Holland

Tyrosine’s Unique Role in the Hierarchical Assembly of Recombinant Spider Silk Proteins: From Spinning Dope to Fibers

Herold H.M., Döbl A., Wohlrab S., Humenik M., Scheibel T.

Designed Spider Silk-Based Drug Carrier for Redox- or pH-Triggered Drug Release

Biomacromolecules 21, 4904-4912

Schwarzer, M. Brehm, J., Vollmer, M., Jasinski, J., Xu, C., Bin Zainiddin, S., Frazöhlilch, T., Schott, M., Greiner, A., Scheibel, T. &Laforsch, C.

Shape, size, and polymer dependent effects of microplastics on Daphnia magna

Hazardous Materials, 436, 2022

Chan, N., Lentz, S., Gurr, P., Tan, S., Scheibel, T. & Qiao G.

Vernetzte Polypeptide durch RAFT-vermittelte Polymerisation zum kontinuierlichen Aufbau von Polymerfilmen

Angewandte Chemie, 2021

Riedl, S., Völkl, M., Holzinger, A., Jasinski, J., Jerome, V., Scheibel, T., Feldhaar, H. & Freitag, R.

In vitro cultivation of primary intestinal cells from Eisenia fetida as basis for ecotoxicological studies

Ecotoxicology, 2021

Koeck, K. S., Salehi, S., Humenik, M. & Scheibel, T.

Processing of Continuous Non-Crosslinked Collagen Fibers for Microtissue Formation at the Muscle-Tendon Interface

Advanced functional Materials, 2021

Ramsperger, A., Jasinski, J., Völkl, M., Witzmann, T., Meinhart, M., Jerome, V., Kretschmer, W., Freitag, R., Senker, J., Fery A., Kress, H., Scheibel, T. & Laforsch, Ch.

Vermeintlich identische Mikroplastikpartikel unterscheiden sich wesentlich in ihren Materialeigenschaften, die Partikel-Zell-Interaktionen und zelluläre Reaktionen beeinflussen.

Hazardous Materials, Jahrgang 425, 05.03.2022

Lechner, A., Trossmann, V. & Scheibel, T.

Impact of Cell Loading of Recombinant Spider Silk Based Bioinks on Gelation and Printability

Macromol. Biosci. 2021, 2100390

Laomeephol, Ch., Vasuratna, A., Ratanavaraporn, J., Kanokpanont, S., Luckanagul, J., Humenik, M. Scheibel, Th. & Damrongsakkul, S.

Auswirkungen von blended Bombyx mori Silk Fibroin und rekombinanten Spider Silk Fibroin Hydrogels auf das Zellwachstum

Polymers 2021, 13, 4182

Sonnleitner, D., Sommer, Ch., Scheibel, T. & Lang, G.

Ansätze zur Hemmung der Biofilmbildung unter Verwendung natürlicher und künstlicher Seidenmaterialien

Matereials Science & Engineering, Jahrgang 131, Dezember 2021

Jasinski, J., Völkl, M., Jérome, V., Scheibel, T. & Freitag, R.

Noxic effects of polystyrene microparticles on murine macrophages and epithelial cells

Scientific Reports 11, online 03.08.2021

Steiner, D., Winkler, S., Heltmann-Meyer, S., Troßmann, V., Fey, T., Scheibel, T., Horch, R. & Arkudas, A.

Enhanced vascularization and de novo tissue formation in hydrogels made of engineered RGD-tagged spider silk proteins in the arteriovenous loop model

Biofabrication, Vol. 14, Number 4

Murugesan, S. & Scheibel, T.

Chitosan-based nanocomposites for medical applications

Journal of Polymer Science, online June 2021

Esser, T. U., Trossmann, V. T., Lentz, S., Engel, F. B. & Scheibel, T.

Designing of spider silk proteins for human induced pluripotent stem cell-based cardiac tissue engineering

Straßburg, St., Bin Zainuddin, S. & Scheibel, Th.

The Power of Silk Technology for Energy Applications

Adv. Energy Mat., online May 2021

Sommer, Ch., Bargel, H., Raßmann, N. & Scheibel, Th.

Microbial repellence properties of engineered spider silk coatings prevent biofilm formation of opportunistic bacterial strains

MRS Communications, Online April 2021

Röber, M., Scheibel, Th. & Börner, H. G.

Toward Activatable Collagen Mimics: Combining DEPSI “Switch” Defects and Template-Guided Self-Organization to Control Collagen Mimetic Peptides

Macromol Biosci, online May 2021

Röber, M., Scheibel, Th. & Börner, H. G.

Toward Activatable Collagen Mimics: Combining DEPSI “Switch” Defects and Template-Guided Self-Organization to Control Collagen Mimetic Peptides

Macromol Biosci, online May 2021

Sommer, Ch., Bargel, H., Raßmann, N. & Scheibel, Th.

Microbial repellence properties of engineered spider silk coatings prevent biofilm formation of opportunistic bacterial strains

Neubauer, V., Kellner, Ch., Gruen, V., Schenk, A. & Scheibel, T.

Recombinant major ampullate spidroin-particles as biotemplates for manganese carbonate mineralization

Multifunct. Materials, 2021, 4 014002

Neubauer, V., Döbl, A. & Scheibel, T.

Silk-based materials for hard tissue engineering

Materials, 2021, 14 (3), 674

Strassburg, St., Mayer, K. & Scheibel, T.

Functionalization of biopolymer fibers with magnetic nanoparticles

Physical Sciences, online Jan. 21

Saric, M., Eisoldt, L., Döring, V. & Scheibel, T.

Interplay of different Major Ampullate spidroins during assembly and implications for fiber mechanics

Advanced Materials, online Jan. 2021

Hofmaier, M., Urban, B., Lentz, S., Borkner, C., Scheibel, T., Fery, A. & Müller, M.

Dichroic Fourier Transform Infrared Spectroscopy characterization of the β-sheet orientation in spider silk films on silicon substrates

Journal of Physical Chemystry, online Jan. 2021

Humenik, M., Winkler, A. & Scheibel, T.

Patterning of protein-based materials

Biopolymers, 2020; online Dec. 2020

Bargel, H., Hopfe, Ch. & Scheibel, T.

Proteinfasern als Hochleistungsmaterial

Biologie in unserer Zeit, 2020, Vol. 50 (6), 434 – 443

Müller, F., Bin Zainuddin, M. S. & Scheibel, T.

Roll-to-Roll production of spider silk nanofiber nonwoven meshes using centrifugal electrospinning for filtration applications

Molecules 2020, 25(23), 5540

Hopfe, Ch., Ospina-Jara, B., Scheibel, Th. & Cabra-Garcı´, J.

Ocrepeira klamt sp. n. (Araneae: Araneidae), a novel spider species from an Andean páramo in Colombia

PLOS One

Neubauer, V. & Scheibel, T.

Spider silk fusion proteins for controlled collagen binding and biomineralization

ACS Biomaterials Science & Engineering 2020 6 (10), 5599-5608

Kumari, S., Lang, G., DeSimone, E., Spengler, C., Trossmann, V., Lücker, S., Hudel, M., Jacobs, K., Krämer, N. und Scheibel, T.

Data for microbe resistant engineered recombinant spider silk protein based 2D and 3D materials

Data in Brief, Vol. 32, Okt.2020

Haynl, C., Vongsvivut, J., Mayer, K., Bargel, H., Neubauer, V., Tobin, M., Elgar, M. & Scheibel, T.

Free‑standing spider silk webs of the thomisid Saccodomus formivorus are made of composites comprising micro‑ and submicron fiber

Sci Rep, 10, 17624 (2020)

Müller, F., Jokisch, S., Bargel, H. & Scheibel, T.

Centrifugal electrospinning enables the production of meshes of ultrathin polymer fibers

ASC Applied Polymer Materials, 2020 2 (11), 4360-4367

Mathilde Lefevre, Patrick Flammang , A. Sesilja Aranko , Markus B. Linder , Thomas Scheibel , Martin Humenik , Maxime Leclercq , Mathieu Surin , Lionel Tafforeau, Ruddy Wattiez, Philippe Leclère, Elise Hennebert

Sea star-inspired recombinant adhesive proteins self-assemble and adsorb on surfaces in aqueous environments to form cytocompatible coatings

Scheibel T., Bell S., Walke S.

S. cerevisiae and sulfur – a unique way to deal with the environment

FASEB J. 11, 917-921

Scheibel T., Buchner J.

Hsp90 proteins – The Hsp90 Family

Guideb. Mol. Chaperones Protein-Folding Catal. 151.

Nichtl A., Buchner J., Jaenicke R., Rudolph R., Scheibel T.

Folding and association of β-galactosidase

J. Mol.Biol. 282, 5, 1083-1091

Thomas Scheibel

Spider silk-based biomaterials: a new opportunity for product development in many industries

Weiss A. C. G., Herold H. M., Lentz S., Faria M., Besford Q. A., Ang C.-S., Caruso F., Scheibel T.

Surface modification of spider silk particles to direct biomolecular corona formation

Kramer J. P. M., Aigner T. B., Petzold J., Roshanbinfar K., Scheibel T., Engel F. B.

Recombinant spider silk protein eADF4(C16)-RGD coatings are suitable for cardiac tissue engineering

Jokisch, S., Bargel, H., Scheibel, T.

Einsatz von Biomaterialien in Filtersystemen – BioFis

In: Bernotat, A. & Berling, J., Prototype Nature

Mertgen A.-S., Trossmann V., Guex A., Maniura-Weber K., Scheibel T., Rottmar M.

Multifunctional biomaterials – Combining material modification strategies for engineering

ACS Appl. Mater. Interface, online first, 0c01893

Murugesan S., Scheibel T.

Copolymer clay nanocomposites for biomedical applications

Adv. Funct. Mater., online first, 1908101

Humenik M., Preiß T., Goedrich S., Papastavrou G., Scheibel T.

Functionalized DNA spider silk nanohydrogels for controlled protein binding and release

Materials Today Bio, 6, 100045

Aigner T. B., Haynl C., Salehi S., O'Connor A., Scheibel T.

Nerve guidance conduit design based on self-rolling tubes

Materials Today Bio, 5, 100042

Salehi S., Koeck K., Scheibel T.

Spider silk for tissue engineering applications

Molecules, 25, 737-757

Fratzl P., Jacobs K., Möller M., Scheibel T., Sternberg K.

Materialforschung – Impulsgeber Natur

acatech Diskussion, 2020

Bruns N., Scheibel T.

Biomimetic Polymers – Editorial

Europ. Polym. J., 122, 109370

Humenik M., Pawar K., Scheibel T.

Nanostructured, self-assembled spider silk materials for biomedical applications

In: S. Perrett et al. (eds.), Biological and Bio-inspired Nanomaterials, (Advances in Experimental Medicine and Biology 1174), 187-221

Borkner C. B., Lentz S., Müller M., Fery A., Scheibel T.

Ultra-thin spider silk films: Insights into spider silk assembly on surfaces

ACS Appl. Polym. Mater., 1, 3366-3374

Kumari S., Bargel H., Scheibel T.

Recombinant spider silk silica hybrid scaffolds with drug releasing properties

Macromol. Rapid Commun., 41, 1900426

Pawar K., Welzel G., Haynl C., Schuster S., Scheibel T.

Recombinant spider silk and collagen-based nerve guidance conduits

ACS Appl. Bio Mater., 2, 4872−4880

DeSimone E., Aigner T. B., Humenik M., Lang G., Scheibel T.

Aqueous electrospinning of recombinant spider silk proteins

Mater. Sci. Eng. C, 106, 110145

Saric M., Scheibel T.

Engineering of silk proteins for materials applications

Curr. Opin. Biotechnol., 60, 213–220

Steiner D., Lang G., Fischer L., Winkler S., Fey T., Greil P., Scheibel T., Horch R. E., Arkudas A.

Intrinsic vascularisation of recombinant eADF4(C16) spider silk matrices in the arteriovenous loop model

Tissue Eng. Part A,  25, 21-22

Aigner T. B., Scheibel T.

Self-rolling refillable tubular enyme containers

ACS Appl. Mater. Interfaces 2019, 11, 15290-15297

Wang J., Suhre M. H., Scheibel, T.

A mussel polyphenol oxidase-like protein shows thiol-mediated antioxidant activity

Europ. Polym. J., 113, 305–312

Jakob U., Scheibel T., Bose S., Reinstein J., Buchner J.

Assessment of the ATP binding properties of Hsp90

J. Biol. Chem. 271, 10035–10041

Scheibel T., Neuhofen S., Weikl T., Mayr C., Reinstein J., Vogel P. D., Buchner J.

ATP binding properties of human Hsp90

J. Biol. Chem. 272, 18608-18613

Scheibel T., Siegmund H. I., Jaenicke R., Ganz P., Lilie H., Buchner J.

The charged region of Hsp90 modulates the function of the N-terminal domain

Proc. Natl. Acad. Sci. U S A. 4, 1297-302

Scheibel T., Buchner J.

The Hsp90 complex – a super-chaperone machine as a novel drug target

Biochem. Pharmacol. 6, 675-682.

Scheibel T., Weikl T., Buchner J.

Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

Proc. Natl. Acad. Sci. U S A. 4, 1495- 1499.

Hardy J. G., Bertin A., Torres‐Rendon J. G., Leal‐Egaña A., Humenik M., Bauer, F., Walther A., Cölfen H., Schlaad H., Scheibel T.

Facile photochemical modification of silk protein-based biomaterials

Macromol. Biosci., 28: 1800216

Roshanbinfar K., Vogt L., Greber B., Diecke S., Boccaccini A. R., Scheibel T., Engel F. B.

Electroconductive biohybrid hydrogel for enhanced maturation and beating properties of engineered cardiac tissues

Adv. Funct. Mater., 28: 1803951

Wang J., Scheibel T.

Coacervation of the recombinant Mytilus galloprovincialis foot protein-3b

Biomacromolecules, 19: 3612 – 3619

DeSimone E., Pellert A., Schacht K., Scheibel T.

Recombinant spider silk-based bioinks

Biofabrication, 9: 044104

Lang G., Herold H., Scheibel T.

Properties of engineered and fabricated silks

 Fibrous Proteins. Structures and Mechanisms. Subcell. Biochem., 82: 527-573

Spieß K., Wohlrab S., Scheibel T.

Structural characterization and functionalization of engineered spider silk films

Soft Matter 6, 4168–4174

Smith M A., Scheibel T.

Functional amyloids used by organisms: A lesson in controlling assembly

Macromol. Chem. Phys. 210, 127-135

Scheibel T.

Herstellung und Anwendung von Spinnenseide

Bionik. Patente aus der Natur 3. Bionik Konferenz. 130-139

Humenik M., Mohrand M., Scheibel T.

Self-assembly of spider silk-fusion proteins comprising enzymatic and fluorescence activity.

Bioconjugate Chem., 29: 898 – 904.

Herold H. M., Aigner T. B., Grill C., Krüger S., Taubert A., Scheibel T.

Spider-MAEN recombinant spider silk based hybrid materials

Bioinspired, Biomimetic Nanobiomater., 8, 99-108

Röber M., Laroque S., Scheibel T., Börner H.-G.

Modulating the collagen triple helix formation by switching: Positioning effects of depsi-defects on the assembly of [Gly-Pro-Pro]7 collagen mimetic peptides

Euro. Polym. J., 112, 301 – 305  

Zha H. R., Delparastan P., Fink D. T., Bauer J., Messersmith P. B., Scheibel T.

Universal nanothin silk coatings via controlled spidroin self-assembly

Biomater. Sci., 2019, 7, 683-695

Molina A., Humenik M., Scheibel T.

Nanoscale patterning of surfaces via DNA directed spider silk assembly

Biomacromol., 20, 347-352

Scheibel T.

Recombinant production of mussel byssus inspired proteins

Biotechnol. J., 13: 1800146

Hofmann E., Krüger K., Haynl C., Scheibel T., Trebbind M., Förster S.

Microfluidic nozzle device for ultrafine fiber solution blow spinning with precise diameter control

LabChip,18, 2225-2234

Golser A. V., Röber M., Börner H. G., Scheibel T.

Engineered Collagen: A redox switchable framework for tunable assembly and fabrication of biocompatible surfaces

ACS Biomater. Sci. Eng., 4: 2106 – 2114

Lucke M., Mottas I., Herbst T., Hotz C., Römer L., Schierling M., Slotta U., Spinetti T., Scheibel T., Winter G. T., Bourquin C., Engert J.

Engineered spider silk hybrid particles as delivery system for peptide vaccines

Biomaterials, 172, 105 – 115   

Kumari S., Bargel H., Anby M. U., Lafargue D., Scheibel T.

Recombinant spider silk hydrogels for sustained release of biologicals

ACS Biomat., 4: 1750 – 1759  

Golser A. V., Scheibel T.

Routes towards novel collagen-like biomaterials

Fibers, 6: 21  

Lintz E. S., Neinhuis C., Scheibel T.

Altering silk film surface properties through Lotus-like mechanisms

Macromol. Mater. Eng., 303: 1700637  

Aigner T. B., DeSimone E., Scheibel T.

Biomedical applications of recombinant silk-based materials

Adv. Mater., 30: 1704636  

Salehi S., Scheibel T.

Biomimetic spider silk fibres: from vision to reality

The Biochemist, 40: 4 – 7

Mickoleit F., Borkner C. B., Toro-Nahuelpan M., Herold, H. M., Maier D. S., Plitzko J. M., Schüler D., Scheibel T.

In-vivo coating of bacterial magnetic nanoparticles by magnetosome expression of spider silk-inspired peptides

Biomacromolecules, 19: 962 – 972  

Haug M., Reischl B., Prölß G., Pollmann C., Buckert T., Keidel C., Schürmann S., Hock M., Rupitsch S., Heckel M., Pöschel T., Haynl C., Kiriaev L., Head S. L., Friedrich O., Scheibel T.

The MyoRobot: A novel automated biomechatronics system to assess voltage/Ca2+ biosensors and ctive/passive biomechanics in muscle and biomaterials

Biosens. Bioelectron., 102: 589 – 599  

Humenik M., Lang G., Scheibel T.

Silk nanofibril self-assembly versus electrospinning

Wiley Interdiscip. Rev.: Nanomed. Nanobiotechnol., 10: e1509  

Bargel H., Scheibel T.

Inspirationen für mechanisch stabile Materialien aus der Natur – Von Gräsern über Spinnenseide bis zu Kieselalge

MNU Journal, 1: 37 – 44

Bargel H., Scheibel T.

Bio-inspirierte Materialien

MNU Journal, 1: 4-10

Jokisch S., Bargel H., Scheibel T.

Einsatz von Biomaterialien in Filtersystemen

In: Prototype Nature 

Wicklein V. J., Singer B. B., Scheibel T., Salehi S.

Nanoengineered biomaterials for corneal regeneration

In: Nanoengineered Biomaterials for Regenerative Medicine. Micro- and Nano Technologies, Elsevier: 379-415

DeSimone E., Schacht K., Alexandra P., Scheibel T.

Recombinant spider silk-based bioinks

Biofabrication 9, 4, 044104  

Anton A. M., Heidebrecht A., Mahmood N., Beiner M., Scheibel T., Kremer F.

Foundation of the outstanding toughness in biomimetic and natural spider silk

Biomacromolecules, 8: 3954 – 3962

Jokisch S., Neuenfeldt M., Scheibel T.

Silk-based fine dust filters for air filtration

Adv. Sustainable Syst., 1: 1700079 doi:10.1002/adsu.201700079

Scheibel T.

Applicability of biotechnologically produced insect silks

Zeitschrift für Naturforschung, 72 , 365-385  

Petzold J., Touska F., Zimmermann K., Scheibel T., Engel B F.

Surface features of recombinant spider silk protein eADF4(κ16)-made materials are well-suited for cardiac tissue engineering

Adv. Funct. Mater., 27: 1701427

Golser A. V., Scheibel T.

Biotechnological production of the mussel byssus derived collagen preColD

RSC Adv., 7: 38273 – 38278  

Thamm C., DeSimone E., Scheibel T.

Characterization of hydrogels made of a novel spider spilk protein eMaSp1s and evaluation for 3D printing

Macromol. Biosci., 11: 1700141

Bauer J., Scheibel T.

Dimerization of the conserved N-terminal domain of a spider silk protein controls the self-assembly of the repetitive core domain

Biomacromolecules, 18: 2521 – 2528  

Neuenfeldt M., Scheibel T.

Sequence identification, recombinant production, and analysis of the self-assembly of egg stalk silk proteins from lacewing Chrysoperla carnea

Biomolecules, 7: 43

Thamm C., Scheibel T.

Recombinant production, characterization, and fiber spinning of an engineered short Major Ampullate Spidroin (MaSp1s)

Biomacromolecules, 18: 1365 – 1372  

Bauer J., Scheibel T.

Conformational stability and interplay of N- and C-terminal domains

Biomacromolecules 2017, 18, 835 – 845

Lang G., Neugirg R B., Kluge D., Fery A., Scheibel T.

Mechanical testing of engineered spider silk filaments

ACS Appl. Mater. Interfaces,9: 892 – 900

Helfricht N., Doblhofer E., Bieber V., Lommes P., Sieber V., Scheibel T., Papastavrou G.

Probing the adhesion properties of alginate hydrogels: a new approach towards the preparation of soft colloidal probes for direct force measurement

Soft Matter. 13: 578 – 589  

Bauer J., Schaal D., Eisold L., Schweimer K., Schwarzinger S., Scheibel T.

Acidic residues control the dimerization of the N-terminal domain of Black Widow spiders’ Major Ampullate Spidroin 1

Sci. Rep. 6, 34442

Doblhofer E., Schmid J., Rieß M., Daab M., Suntinger M., Habel C., Bargel H., Hugenschmidt C., Rosenfeldt S., Breu J., Scheibel T.

Structural insights into water-based spider silk protein-nanoclay composites with excellent gas and water vapor barrier properties

Appl. Mater. Interfaces. 8, 25535 – 25543

Helfricht N., Doblhofer E., Duval L F J., Scheibel T., Papastavrou G.

Colloidal properties of recombinant spider silk protein particles

J. Phys. Chem. C. 120, 18015 – 18027  

Schierling B M., Doblhofer E., Scheibel T.

Cellular uptake of drug loaded spider silk particles

Biomater. Sci. 4: 1515-1523

Borkner B C., Wohlrab S., Lang G., Scheibel T.

Surface modification of polymeric biomaterials using recombinant spider silk proteins

ASC Biomat. Sci.Eng. 3, 767 – 775

Haynl C., Hofmann E., Pawar K., Förster S., Scheibel T.

Microfluidics-produced collagen fibers show extraordinary mechanical properties

Nano Lett.16: 5917 – 5922

DeSimone E., Schacht K., Scheibel T.

Cations influence the crosslinking of hydrogels made of recombinant, polyanionic spider silk proteins

Mater. Lett., 183: 101-104

Schacht K., Vogt J., Scheibel T.

Foams made of engineered recombinant spider silk proteins

ACS Biomater. Sci. Eng. 2: 517-525  

Schaal D., Bauer J., Schweimer K., Scheibel T., Rösch P., Schwarzinger S.

Resonance assignment of an engineered amino-terminal domain of a major ampullate spider silk with neutralized charge cluster

Biomol. NMR Assign. 10: 199-202

Peng L., Jiang S., Seuß M., Fery A., Lang G., Scheibel T., Agarwal S.

Two-in-one composite fibers with side-by-side arrangement of silk fibroin and poly(L-lactide) by electrospinning

Macromol. Mater. Eng. 301: 48-55

Caplan L D., Scheibel T.

Recombinant Silk Production in Bacteria

Ref. Module in Materials Science and Engineering.8, 803581-802274

Bauer J., Scheibel T.

Die Schwarze Witwe und ihre Künste

UBT Aktuell, 2: 60 – 63

Bargel H., Scheibel T.

Zukunftsfeld Bionik

UBT Spektrum, 1: 54 – 57

Jüngst T., Smolan W., Schacht K., Scheibel T., Groll J.

Strategies and molecular design criteria for 3D printable hydrogels

Chem. Rev., 116: 1496-1539

Scheibel T., Groll J., Boccaccini R A., Zehnder T., Jüngst T., Schacht K.

Zellgewebe aus dem Drucker

Nachrichten aus der Chemie, 64: 13-16

Zahn H., Krasowski A., Scheibel T.

Silk

Ullmann’s Encycl. Ind. Chem.

Humenik M., Smith A M., Arndt S., Scheibel T.

Data for ion and seed dependent fibril assembly of a spidroin core domain

Data in Brief, 4: 571–576

Humenik M., Smith A., Arndt S., Scheibel T.

Ion and seed dependent fibril assembly of a spidroin core domain

J. Struct. Biol. 191: 130–138

Herrmann M S., Scheibel T.

Enzymatic degradation of films, particles and non-woven meshes

ACS Biomater. Sci. Eng., 1: 247–259

Heidebrecht A., Eisoldt L., Johannes D., Schmidt A., Geffers M., Lang G., Scheibel T.

Biomimetic fibers made of recombinant spidroins with the same toughness as natural spider silk

Adv. Mater., 27: 2189–2194  

Schacht K., Jüngst T., Schweinlin M., Ewald A., Groll J., Scheibel T.

Biofabrication of cell-loaded 3D spider silk constructs

Angew, Chem., 54: 2816–2820

Elsner B M., Herold M H., Herrmann M S., Bargel H., Scheibel T.

Enhanced cellular uptake of engineered spider silk particles

Biomater. Sci., 3: 543–551

Doblhofer E., Scheibel T.

Engineering of recombinant spider silk proteins allows defined uptake and release of substances

J. Pharm. Sci, 104: 988-994

Scheibel T.

Die Kräfte von Superhelden – Oder: Was Spiderman besser wissen sollte

Vorlesungsreihe KinderUniversität Bayreuth SS .

Scheibel T.

Vom Spinnennetz zur High-Tech-Faser

Naturwiss. Rundschau.. 68: 524-525

Jungst T., Smolan W., Schacht K., Scheibel T., Groll J.

Strategies and molecular design criteria for 3D printable hydrogels

Chem. Rev.. 99: 9361-9380

Doblhofer E., Heidebrecht A., Scheibel T.

To spin or not to spin: spider silk fibers and more

Appl. Microbiol. Biotechnol. 99: 9361-9380  

DeSimone E., Schacht K., Jungst T., Groll J., Scheibel T.

Biofabrication of 3D constructs: fabrication technologies and spider silk proteins as bioinks

Pure Appl. Chem., 87: 737–749

Scheibel T.

Engineering of rec SSP allows defined drug uptake and release

TechConnect Briefs: Biotech, Biomaterials, and Biomedical 1-4

Zeplin H P., Berninger K A., Maksimovikj C N., Gelder V P., Scheibel T., Walles H.

Verbesserung der Biokompatibilität von Silikonimplantaten

Handchir. Mikrochir. Plast. Chir., 46: 336-41  

Lauterbach Y A., Scheibel T.

Life cycle assessment of spider silk nonwoven meshes in an air filtration device

Green Materials., 3: 15-24

Humenik M., Markus D., Scheibel T.

Controlled hierarchical assembly ofspider silk-DNA chimeras into ribbons and raft-like morphologies

Nano Lett.., 14, 3999−4004

Humenik M., Magdeburg M., Scheibel T.

Influence of repeat numbers on self-assembly rates of repetitive recombinant spider silk proteins

J. Struct. Biol., 186, 431-437

Suhre.H M., Steegborn C., Gertzb M., Scheibel T.

Crystallization and preliminary X-ray diffraction analysis os PTMP1

Acta. Cryst. Sec. 70, 769-772

Hardy J G., Pfaff A., Egaña-L A., Müller A H., Scheibel T.

Glycopolymer functionalization of engineered spider silk protein based materials for improved cell adhesion

Macromol. Biosci., 14, 936-42

Suhre M H., Gertz M., Steegborn C., Scheibel T.

Structural and functional features of a collagen-binding matrix protein from the mussel byssus

Nat. Comm., 5, 3392

Pinto-S D J R., Lamprecht G., Chen W Q., Heo S., Hardy J G., Priewalder H., Scheibel T., Palma M S., Lubec G.

Structure and post-translational modifications of the web silk protein spidroin-1 from Nephila spiders

J. Prot., 105, 174–185

Zeplin.H P., Maksimovikj C N., Jordan C M., Nickel J., Lang G., Axel H., Römer L., Scheibel T.

Spider silk coatings as a bioshield to reduce periprosthetic fibrous capsule formation

Adv. Funct. Mater. 24, 2658–2666

Humenik M., Scheibel T.

Nanomaterial building blocks based on spider silk–oligonucleotide conjugates

ACS Nano 8, 1342-1349

Heidebrecht A., Scheibel T.

Spionik – Biotech Spinnenseide und ihre Einsatzgebiete

GIT Bioforum 2, 20-22

Humenik M., Scheibel T.

Self-assembly of nucleic acids, silk and hybrid materials thereof

J. Phys. Condens. Matter 26, 503102

Zollfrank C., Scheibel T., Seitz H., Travitzky N.

Bioinspired materials engineering

Ullmann’s Encycl. Ind. Chem.

Borkner B C., Elsner B M., Scheibel T.

Coatings and films made of silk proteins

Appl. Mater. Interface. 29, 62-69  

Lang G., Scheibel T.

Multifunktionale Spinnenseide – ein vielversprechender Werkstoff

MaschinenMarkt 26, 36-39

Schacht K., Scheibel T.

Processing of recombinant spider silk proteins into tailor-made materials for biomaterials applications

Curr. Opin. Biotechnol. 29, 62-69

Hagenau A., Suhre H M., Scheibel T.

Nature as a blueprint for polymer material concepts: protein fiber-reinforced composits as holdfasts of mussels

Progr. Polym. Sci. 39, 1564-1583

Scheibel T.

Die Natur als Vorbild für bioinspirierte Materialien der Zukunft

TIB  33-36 

Neuenfeldt M., Scheibel T.

Silks From Insects – From Natural Diversity to Application

Insect Molecular Biology and Ecology, 376-400

Keerl D., Scheibel T.

Rheological characterization of silk solutions

Green Materials, 2, 11 –23  

Heim M., Elsner M B., Scheibel T.

Lipid-specific ß-sheet formation in a mussel byssus protein domain

Biomacromolecules, 14, 3238-3245  

Blüm C., Nichtl A., Scheibel T.

Spider silk capsules as protective reaction containers for enzymes

Adv. Funct. Mater., 24, 763–768  

Bauer F., Wohlrab S., Scheibel T.

Controllable cell adhesion, growth and orientation on layered silk protein films

Biomater. Sci., 1, 1244-1249  

Helfricht N., Klug M., Mark A., Kuznetsov V., Blüm C., Scheibel T., Papastavrou G.

Surface properties of spider silk particles in solution

Biomater. Sci, 1, 1166-1171  

Neubauer P. M., Blüm C., Agostini E., Engert J., Scheibel T., Fery A.

Micromechanical characterization of spider silk particles

Biomater. Sci., 1, 1160-1165  

Hardy J. G., Leal-Egaña A., Scheibel T.

Engineered spider silk protein-based composites for drug delivery

Macromol. BioSci., 13, 1431–1437  

Claussen K. U., Lintz E. S., Giesa R., Schmidt H. W., Scheibel T.

Protein gradient films of fibroin and gelatine

Macromol. BioSci., 13, 1396–1403  

Lang G., Jokisch S., Scheibel T.

Air filter devices including nonwoven meshes of electrospun recombinant spider silk proteins

J. Vis. Exp., 75, e50492  

Hofmann J. P., Denner P., Krammer N. C., Kuhn P. H., Suhre M. H., Scheibel T., Lichtenthaler S. F., Schätzl H. M., Bano D., Vorberg I. M.

Cell-to-cell propagation of infectious cytosolic protein aggregates

Proc. Natl. Acad. Sci. U S A., 110, 5951–5956  

Scheibel T.

Spinnenseide – Biotechfaser mit naturidentischer Belastbarkeit

Chemie & More, 4, 3-5

Lintz E. S., Scheibel T.

Dragline, egg stalk, and byssus – A comparison of outstanding protein fibers

Adv. Funct. Mater., 23, 4467–4482  

Heidebrecht A., Scheibel T.

Recombinant production of spider silk proteins

Adv. Appl. Microbiol. 82, 115-153  

Wohlrab S., Thamm C., Scheibel T.

The Power of Recombinant Spider Silk Proteins

In: Biotechnology of Silk (Eds Asakura T., Miller T.), 179-201

Lauterbach A. Y., Scheibel T.

Determining the Environmental Benefit of Artificial Spider Silk Products

NSTI-Nanotech., 3, 108-111  

Smith A., Scheibel T.

Hierarchical Protein Assemblies as a Basis for Materials

In: Materials Design Inspired by Nature: Function Through Inner Architecture (Eds. Fratz P., Dunlop J. W. C., Weinkamer R.), 256-281  

Bauer F., Bertinetti L., Masic A., Scheibel T.

Dependence of mechanical properties of lacewing egg stalks on relative humidity

Biomacromolecules. 13, 3730-3735

Wohlrab S., Spießa K., Scheibel T.

Varying surface hydrophobicities of coatings made of recombinant spider silk proteins

J. Mater. Chem. 22, 22050-22054

Young L S., Gupta M., Hanske C., Fery A., Scheibel T., Tsukruk V V.

Utilizing conformational changes for patterning thin films of recombinant spider silk proteins

Biomacromol. 13, 10, 3189-3199

Wohlrab S., Müller S., Schmidt A., Neubauer S., Kessler H., Egaña-L A., Scheibel T.

Cell adhesion and proliferation on RGD-modified recombinant spider silk proteins

Biomaterials 33, 6650-6659

Egañaa-L A., Scheibel T.

Interactions of cells with silk surfaces

J. Mater. Chem. 22, 14330-14336

Bauer F., Scheibel T.

Artificial egg stalks made of a recombinantly produced lacewing silk protein

Ang. Chemie Intl. Edit. 124, 6627-6630

Keerl D., Scheibel T.

Characterization of natural and biomimetic spider silk fibers

Bioinspired, Biomimetic Nanobiomater.1, 83-94

Egaña-L A., Lang G., Mauerer C., Wickinghoff J., Weber M., Geimer S., Scheibel T.

Interactions of fibroblasts with different morphologies made of an engineered spider silk protein

Adv. Eng. Mater. 14, B67-B75

Bluem C., Scheibel T.

Control of drug loading and release properties of spider silk sub-microparticles

BioNanoSci. 2, 67-74

Claussen K U., Giesa R., Scheibel T., Schmidt H W.

Learning from nature: synthesis and characterization of longitudinal polymer gradient materials inspired by mussel byssus threads

Macromol. Rapid Commun. 33, 206-211

Claussen K U., Scheibel T., Schmidt H W., Giesa R.

Polymer gradient materials: can nature teach us new tricks?

Macromol. Mater. Eng. 297, 938–957

Eisoldt L., Thamm C., Scheibel T.

The role of terminal domains during storage and assembly of spider silk proteins

Biopolymers. 97, 355-361

Slotta U., Hess S., Spieß K., Stromer T., Serpell L., Scheibel T.

Spider silk and amyloid fibrils: A structural comparison

Macromol. Biosci. 7, 73-90

Spiess K., Ene R., Keenan C D., Senker J., Kremerb F., Scheibel T.

Impact of initial solvent on thermal stability and mechanical properties of recombinant spider silk films

J. Mater. Chem. 21, 13594-13604

Schacht K., Scheibel T.

Controlled hydrogel formation of a recombinant spider silk protein

Biomacromol. 12, 2488–2495  

Hagenaua A., Papadopoulos P., Kremer F., Scheibel T.

Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads

J. Structural Biol. 175, 339-347

Lammel A., Schwab M., Hofer M., Winter G., Scheibel T.

Recombinant spider silk particles as drug delivery vehicles

Biomaterials 32, 2233–2240

Hagn F., Thamm C., Scheibel T., Kessler H.

pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk – Implications for fiber formation

Angew. Chem. Int. Ed. 50, 310-313

Humenik M., Smith A., Scheibel T.

Recombinant spider silks – biopolymers with potential for future applications

Polymers 3, 640–661

Spiess K., Lammel A., Scheibel T.

Recombinant spider silk proteins for applications in biomaterials

Macromol.Biosci. 2011, S32-S41

Eisoldt L., Smith A., Scheibel T.

Decoding the secrets of spider silk

Materials Today. 14, 80–86

Humenik M., Scheibel T., Smith A.

Spider Silk: Understanding the Structure–Function Relationship of a Natural Fiber

Prog. Mol. Biol. Transl. Sci. 103, 131-185.

Spieß K., Wohlrab S., Scheibel T.

Structural characterization and functionalization of engineered spider silk films

Soft Matter.6, 4168–4174

Keerl D., Hardy J G., Scheibel T.

Biomimetic spinning of recombinant silk proteins

Mater. Res. Soc. Symp. Proc.07-20, 1239.

Hagn F., Eisoldt L., Hardy J G., Vendrely C., Coles M., Scheibel T., Kessler H.

A conserved spider silk domain acts as a molecular switch that controls fibre assembly

Nature 365, 239-242

Lammel A S., Hu X., Park S H., Kaplan D L., Scheibel T.

Controlling silk fibroin particle features for drug delivery

Biomaterials. 31, 4583-4591

Hagenau A., Scheibel T.

Towards the recombinant production of mussel byssal collagens

J. Adhesion. 86, 10-24

Eisoldt L., Hardy J G., Heim M., Scheibel T.

The role of salt and shear on the storage and assembly of spider silk proteins.

J. Struct. Biol. 170, 413–419

Heim M., Ackerschott C B., Scheibel T.

Characterization of recombinantly produced spider flagelliform silk domains

J. Struct. Biol. 170, 420–425

Scheibel T.

Spider silk from nature to bio-inspired materials

Chem. Fiber. Int. 3, 15-16

Scheibel T.

Advanced Biomaterials

Macromol. Biosciences. 10, 674

Spiess K., Lammel A., Scheibel T.

Recombinant spider silk proteins for applications in biomaterials

Macromol. Biosciences. 10, 998-1007

Hardy J G., Scheibel T.

Composite materials based on silk proteins

Progr. Polymer Sci. 35, 1093-1115

Egaña-L A., Scheibel T.

Silk-based materials for biomedical applications

Biotechnol. Appl. Biochem. 55, 155–167

Heim M., Römer L., Scheibel T.

Hierarchical structures made of protein.The complex architecture of spider webs and their constituent silk proteins

Chem. Soc. Rev.39, 156–164

Suhre M H., Hess S., Golser A V., Scheibel T.

Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM

J. Inorg. Biochem. 120, 1711-1720

Vézy C., Hermanson.D K., Scheibel T., Bausch A R.

Interfacial rheological properties of recombinant spider-silk proteins

Biointerphases 4, 43-46

Pirzer T., Geisler M., Scheibel T., Hugel T.

Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion

Physical Biol. J. 6, 025004

Krammer C., Kryndushkin D., Suhre M H., Kremmer E., Hofmann A., Pfeifer A., Scheibel T., Wickner R B., Schätzl H M., Vorberg I.

The yeast Sup35NM domain propagates as a prion in mammalian cells

Proc. Natl. Acad. Sci. USA 106, 462-467

Hagenau A., Scheidt H A., Serpell L., Huster D., Scheibel T.

Structural analysis of proteinaceous components in byssal threads of the mussel Mytilus galloprovincialis

Macromol. Biosciences 9, 162-168

Smith A M., Scheibel T.

Functional amyloids used by organisms: A lesson in controlling assembly

Macromol. Chem. Phys. 210, 127-135

Hardy J G., Scheibel T.

Silk-inspired polymers and proteins

Biochem. Soc. Trans. 37, 677–681

Hardy J G., Scheibel T.

Production and processing of spider silk proteins

J. Polymer. Sci. Part.A: Polymer. Chem. 47, 3957–3963

Grunwald I., Rischka K., Kast S M., Scheibel T., Bargel H.

Mimicking biopolymers on a molecular scale: Nano(bio)technology based on engineered protein

Phil. Trans. Roy. Soc. London: A 367, 1727-1747

Heim M., Römer L., Scheibel T.,

Hierarchical structures made of protein. The complex architecture of spider webs and their constituent silk protein

Chem. Soc. Rev. 39, 156–164

Römer L., Scheibel T.

The elaborate structure of spider silk: Structure and function of a natural high performance fiber

Prion 2, 154-161

Scheibel T

Spinnenseide: Was Spiderman wissen sollte

Biospektrum

Heim M., Keerl D., Scheibel T.

Spider Silk: From Soluble Protein to Extraordinary Fibers

Angew. Chem. Int. Edit. 48, 3584-3596

Liebmann B., Hümmerich D., Scheibel T, Fehr M.

Formulation of poorly water-soluble substances using self-assembling spider silk protein

Colloids Surf., A 331, 126-132

Slotta U.K., Rammensee S., Gorb S., Scheibel T.

An engineered spider silk protein forms microspheres

Angew. Chem. Int. Ed. 47, 4592-459

Lammel A., Schwab M., Slotta U.K., Winter G., Scheibel T.

Processing conditions for spider silk microsphere formation

ChemSusChem 5, 413-416

Rammensee S., Slotta U.K, Scheibel T., Bausch A.R.

Assembly mechanism of recombinant spider silk proteins

Proc. Natl. Acad. Sci. USA. 105, 6590-6595

Horinek D., Serr A., Geisler M., Pirzer T., Slotta U.K., Lud S.Q., Garrido J.A., Scheibel T., Hugel T., Netz R.R.

Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces

Proc. Natl. Acad. Sci. USA. 105, 2842-2847

Geisler M., Pirzer T., Ackerschott C., Lud S., Garrido A.J., Scheibel T., Hugel T.

Hydrophobic and Hofmeister effects on the adhesion of spider silk proteins onto solid substrates: An AFM-based single-molecule study

Langmuir 24, 1350-1355

Krammer C., Suhre M.H., Kremmer E., Diemer C., Hess S., Schätzl H.M., Scheibel T., Vorberg I.

Prion protein/protein interactions: Fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells

FASEB J. 22, 762-773

Hardy J., Römer L ., Scheibel T.

Polymeric materials based on silk proteins

Polymer 49, 4309-4327

Römer L., Scheibel T.

Spinnen wie die Spinnen

Nachrichten a. d. Chem. 56, 516-519

Scheibel T., Weidenauer U.

Spinnenseidenproteine als pharmazeutischer Hilfsstoff

Dtsch. Apoth. Ztg. 48, 29.

Lammel A., Keerl D., Römer L., Scheibel T.

Proteins: Polymers of natural origin

In: J. Hu (Ed.), Recent Advances in Biomaterials Research, 1-22

Vendrely C., Ackerschott C., Römer L., Scheibel T.

Molecular design of performance proteins with repetitive sequences: Recombinant flagelliform spider silk as basis for biomaterials

Methods. Mol. Biol. 474, 3-14.

Hermanson K D., Harasim M B., Scheibel T., Bausch A R.

Permeability of silk microcapsules made by the interfacial adsorption of protein

Phys. Chem. Chem. Phys. 9, 6442-6446

Hess S., Lindquist S., Scheibel T.

Alternate assembly pathways of the amyloidogenic yeast prion determinant Sup35p-NM

EMBO Rep. 8,1196-1201

Scheibel T, Römer L., Spieß K., Slotta U.

Transparente Folien aus Spinnenseide – Ein Hocheistungsmaterial aus der Natur in neuem Gewand

GIT Labor-Fachz. 11, 928-931

Dong J., Bloom D J., Goncharov V., Chattopadhyay M., Millhauser L G., Lynn G D., Scheibel T., Susan L.

Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions

J. Biol. Chem. 282, 47, 34204–34212

Metwalli E., Slotta U., Darko C., Roth S V., Scheibel T., Papadakis C M.

Structural changes of thin films from recombinant spider silk proteins upon post treatment

Appl. Phys. A. 89, 655-661

Schmidt M., Romer L., Strehle M., Scheibel T.

Conquering isoleucine auxotrophy of Escherichia coli BLR(DE3) to recombinantly produce spider silk proteins in minimal media

Biotechnol. Lett. 29, 1741-1744

Hermanson K D., Huemmerich D., Scheibel T., Bausch A R.

Engineered microcapsules made of reconstituted spider silk

Adv. Mater. 19, 1810-1815

Exler J H., Hümmerich D., Scheibel T.

The amphiphilic properties of spider silks are important for spinning

Angew. Chem. Int. Edit. 46, 3559-3562

Slotta U., Hess S., Spiess K., Stromer T., Serpell L., Scheibel T.

Spider silk and amyloid fibrils – a structural comparison

Macromol. Biosci. 7, 183-188

Lodderstedt G., Hess S., Hause G., Scheuermann T., Scheibel T., Schwarz E.

Effect of OPMD-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1

FEBS.J.274, 2, 346-355.

Römer L., Scheibel T.

Grundlagen für neue Materialien – Seidenproteine

Chemie i. u. 41, 306-314

Vendrely C., Scheibel T.

Biotechnological production of spider silk proteins enables new applications

Macromol Biosci. 7, 4, 401-409.

Scheibel T., Roemer L.

Herstellung und Anwendung von Spinnenseide

 Bionik: Patente aus der Natur, 3, 130-139

Sen Gupta S., Scheibel T.

Folding, self-assembly and conformational switches of proteins.

Protein Folding-Misfolding: Some Current Concepts of Protein Chemistry, 1-33

Slotta U., Tammer M., Kremer F., Koelsch P., Scheibel T.

Structural analysis of films cast from recombinant spider silk proteins

Supramol. Chem. 18, 465-471

Rammensee S., Huemmerich D., Hermanson K., Scheibel T., Bausch A.

Rheological characterisation of recombinant spider silk nanofiber networks

Appl. Phys. A. 82, 261-264

Junghans F., Morawietz M., Conrad U., Scheibel T., Heilmann A., Spohn U.

Preparation and mechanical properties of layers made of recombinant spider silk proteins and silk from silk worm

Appl. Phys. A. 82, 253-260

Zbilut J P., Scheibel T., Huemmerich D., Webber C L., Colafranceschi M., Giuliani A.

Statistical approaches for investigating silk properties

App. Phy. A.  82, 2, 243–251

Huemmerich D., Slotta U., Scheibel T.

Processing and modification of films made from recombinant spider silk proteins

Appl. Phys. A.  82, 219-222

Scheibel T.

Editorial: Silk–a biomaterial with several facets

Appl. Phys. A 82, 191-192

Scheibel T., Buchner J.

Protein Aggregation as a Cause for Disease

Handb. Exp. Pharmacol. 199-219

Scheibel T., Vendrely C.

Mammalian Versus Yeast Prions – Biophysical Insights in Structure and Assembly Mechanisms

Prions: New Res. pp. 251-284

Zbilut J P., Scheibel T., Huemmerich D., Webber C L., Colafranceschi M., Giuliani A.

Spatial stochastic resonance in protein hydrophobicity

Phys. Lett. A. 346, 33-41

Junger A., Kaufmann D., Scheibel T., Weberskirch R.

Biosynthesis of an elastin-mimetic polypeptide with two different chemical functional groups within the repetitive elastin fragment

Macromol. Biosciences 5, 494-501

Scheibel T.

Protein fibers as performance proteins: new technologies and applications

Curr. Opin. Biotech. 16, 427-433

Scheibel T., Serpell L.

Methods to study fibril formation

Protein Folding Handb.Vol. II, pp. 193-249

Huemmerich D., Scheibel T., Vollrath F., Cohen S., Gat U., Ittah S.

Novel assembly properties of recombinant spider dragline silk protein

Curr. Biol. 14, 2070-2074

Huemmerich D., Helsen C W., Quedzuweit S., Oschmann J., Rudolph R., Scheibel T.

Primary structure elements of dragline silks and their contribution to protein solubility and assembly

Biochem. 43, 13604-13612

Scheibel T., Bloom J., Lindquist S L.

The elongation of yeast prion fibers involves separable steps of association and conversion

Proc. Natl. Acad. Sci. USA 101, 2287-2292

Scheibel T.

Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins

Microb. Cell Fact. 3, 14-21

Scheibel T., Buchner J.

Book Review: Methods in Molecular Biology, Vol. 232: Protein Misfolding and Disease: Principles and Methods

Chem.Bio.Chem. 5, 1153-1154

Scheibel T.

Amyloid formation of a yeast prion determinant

J. Mol. Neurosci. 23, 13-22

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