Biofabrication processing / 3D printing
The focus of the research group biofabrication and 3D-printing is on the one hand the analysis of suitable structural proteins to be used as scaffolds for tissue engineering approaches, and on the other hand the development of new, cell-friendly bioinks. In particular, recombinant spider silk proteins are modified dependent on their application and are processed into films, hydrogels, foams, non-woven meshes and nanofibers with defined structure and controlled topography.
Biofabrication is an emerging field in the area of biomaterials, which aims to generate 3D biocompatible constructs using natural materials as building blocks in combination with cells. This approach requires materials recapitulating native tissue properties like in bone, ligament, skin and nerve regeneration. Defined 3D structures, tissue-related hierarchical morphology, and adjusted biochemical composition are important characteristics of a scaffold. To achive this, 3D bioprinting (3DBP) shows particular promise due to precise positioning of scaffold components in three dimensions. Therefore, suitable bioinks are necessary, which are on the one hand printable and on the other hand cytocompatible. Hence, for instance spider silk, collagen, hyaluronic acid, cellulose and alginate are used.
Research Projects
Koeck, Kim (M.Sc.)
kim.koeck(.at.)bm.uni-bayreuth.de
0921-55 6707
Tissue engineering of fibrous tissues of the musculoskeletal system, such as tendon, presents a major challenge for biomedical research due to its complex architecture and mechanical behavior. Natural healing of tendon is limited due to a low number of cells and its avascularity. In healing, a hierarchically organized structure is replaced by a disorganized fibrous scar tissue with inferior mechanical properties. To address this problem, fabric-like braided polymer ropes are used as partial tendon replacements, however, these tend to be inferior due to a lack of biological function as well as lack of material/mechanical gradients. This projects aims to create a total tendon replacement based on a gradient fiber-reinforced composite by combining a textile approach with abio-inspired materials approach. The tendon-like replacement tissue will be evaluated based on the mechanical stability and biocompatibility.
Trossmann, Vanessa (M.Sc.)
vanessa.trossmann(.at.)bm.uni-bayreuth.de
0921-55 7349
Due to its unique mechanical and biochemical properties spider silk is in the focus of research since decades. Spider silk proteins are biodegradable, biocompatible and show no immune reaction in the human body, thereby representing a suitable material for biomedical applications. The development of recombinant technologies, inspired by the natural occurring gene sequences of the European garden spider Araneus diadematus, enable the biotechnological production of spider silk proteins in high-yields. They can be processed into several different morphologies, such as fibers, films, hydrogels, foams, nonwovens and particles, leading to diverse potential applications. With respect to tissue engineering and regenerative medicine, specific cell adhesion is a decisive factor. Since cell attachment to unmodified silk protein is often low, it is sometimes necessary to develop proteins including cell-interacting ligands. The project objective is thus to modify and functionalize biocompatible spider silk scaffolds for guided cell-substrate-interaction by using genetic or chemical coupling and varying processing methods.
Neubauer, Vanessa (M.Sc.)
vanessa.neubauer(.at.)bm.uni-bayreuth.de
0921-55 7343
Among the great challenges of modern medicine is the regeneration of tissues. One promising approach is the manufacturing of tailor-made tissue scaffolds for regenerative medical approaches, known as tissue engineering. Spider silk is a suitable candidate for biomaterial applications since it shows no immunogenicity, good biocompatibility and biodegradability. By processing recombinant spider silk proteins into hydrogels, 3D scaffolds can be printed for biomedical applications. In this context, specialized scaffold preparation for tissue regeneration applications such as gradient materials for tendon replacement are in the focus. This also includes oriented biomineralization of the gradient material similar to the natural blueprint.
Biofabrication, the simultaneous assembly of cells and materials into tissue-like constructs, has significantly gained attention in recent years as an alternative approach to traditional tissue engineering techniques. Within this field, 3D bioprinting (3DBP) shows particular promise due to the ability of precise placement of scaffold components in three dimensions. However, 3DBP is limited to (1) a micron-scale resolution and (2) a narrow range of process-compatible materials being cell-friendly, i.e. ‘bioinks’. Recombinant spider silk proteins have low immunogenicity, and can be processed into several morphologies with tunable mechanical properties, including electrospun fibers and hydrogels. Therefore, it is proposed that recombinant spider silk proteins fabricated into tissue-like constructs by a hybridized 3DBP-electrospinning system will be suitable for regenerative medicine applications. The objectives of this research will be to (1) hybridize a 3D bioprinter with other processing devices and (2) develop novel bioinks based on recombinant spider silk proteins.
Publications
,
, Parthasarathy R, Sawicki G, Lin X-M, Jaeger H, Lindquist S
Conducting nanowires built by controlled self assembly of amyloid fibers and selective metal deposition
Proc. Natl. Acad. Sci. USA 100, 4527-4532
,
Amyloid formation of a yeast prion determinant
J. Mol. Neurosci. 23, 13-22
, Buchner J
Methods in Molecular Biology, Vol. 232: Protein Misfolding and Disease – Principles and Methods.
ChemBioChem. 5, 1153-1154
,
Spider silks: recombinant synthesis, assembly, spinning, and engineering of synthetic proteins
Microbial Cell Factories 3, 14-21
, Bloom J, Lindquist SL
The elongation of yeast prion fibers involves separable steps of association and conversion
Proc. Natl. Acad. Sci. USA 101, 2287-2292
, Huemmerich D, Helsen CW, Quedzuweit S, Oschmann J, Rudolph R,
Primary structure elements of dragline silks and their contribution to protein solubility and assembly
Biochemistry 43, 13604-13612
, Huemmerich D, Vollrath F, Cohen S, Gat U, Ittah S
Novel assembly properties of recombinant spider dragline silk protein
Curr. Biol. 14, 2070-2074
, Serpell L
Methods to study fibril formation
In: J. Buchner & T. Kiefhaber (eds.):Handbook of protein folding Vol. II, pp. 193-249 Wiley VHC, Weinheim
,
Protein fibers as performance proteins: new technologies and applications
Curr. Opin. Biotech. 16, 427-433
, Junger A, Kaufmann D
Biosynthesis of an elastin-mimetic polypeptide with two different chemical functional groups within the repetitive elastin fragment
Macromol. Biosciences 5, 494-501
, Zbilut J.P, Huemmerich D, Webber C.L , Colafranceschi M, Giuliani A
Spatial stochastic resonance in protein hydrophobicity
Phys. Lett. A 346, 33-41
, Vendrely C
Mammalian Versus Yeast Prions – Biophysical Insights in Structure and Assembly Mechanisms
In: B.V. Doupher (ed.): Trends in Prion research, pp. 251-284 Nova Publisher
, Buchner J
Protein Aggregation as a Cause for Disease
,
Editorial: Silk–a biomaterial with several facets
Appl. Phys. A 82, 191-192
, Huemmerich D, Slotta U
Processing and modification of films made from recombinant spider silk proteins
Appl. Phys. A 82, 219-222
, Zbilut J.P, Huemmerich D, Webber, C.L, Colafranceschi M, Giuliani A.
Statistical approaches for investigating silk properties
, Rammensee S, Huemmerich D, Hermanson K, Bausch A.
Rheological characterisation of recombinant spider silk nanofiber networks
Appl. Phys. A 82, 261-264
, Slotta U, Tammer M, Kremer F, Koelsch P
Structural analysis of films cast from recombinant spider silk proteins
Supramol. Chem. 18, 465-471
, Sen Gupta, Sayam
Folding, self-assembly and conformational switches of proteins.
.Protein Folding-Misfolding: Some Current Concepts of Protein Chemistry, pp. 1-33 Nova Publisher
, Roemer, L
Herstellung und Anwendung von Spinnenseide
A. Kesel, D. Zehren (eds.): Bionik: Patente aus der Natur,. 3. Bionik Konferenz 2006, Bremen, pp. 130-139
, Vendrely C
Biotechnological production of spider silk proteins enables new applications
Macromol. Biosciences 7, 401-409
, Römer L
Grundlagen für neue Materialien – Seidenproteine
Chemie i. u. Zeit 41, 306-314
, Lodderstedt G, Hess S, Hause G, Scheuermann T, Schwarz E.
Effect of OPMD-associated extension of seven alanines on the fibrillation properties of the N-terminal domain of PABPN1
, Slotta U, Hess S, Spiess K, Stromer T, Serpell L
Spider silk and amyloid fibrils – a structural comparison
Macromol. Biosciences 7, 183-188
, Exler JH, Hümmerich D
The amphiphilic properties of spider silks are important for spinning
Angew. Chem. Int. Edit. 46, 3559-3562
, K. D. Hermanson , D. Huemmerich, A. R. Bausch
Engineered microcapsules made of reconstituted spider silk
Adv. Mater. 19, 1810-1815
, Schmidt M , Romer L, Strehle M
Conquering isoleucine auxotrophy of Escherichia coli BLR(DE3) to recombinantly produce spider silk proteins in minimal media
Biotechnol. Lett. 29, 1741-1744
, E. Metwalli, U. Slotta, C. Darko SV. Roth, C.M. Papadakis
Structural changes of thin films from recombinant spider silk proteins upon post treatment
Appl. Phys. A 89, 655-661
, Jijun Dong , Jesse D. Bloom , Vladimir Goncharov , Madhuri Chattopadhyay , Glenn L. Millhauser, David G. Lynn ,and Susan Lindquist,
Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions
, Dr. Lin Römer , Kristina Spieß
Transparente Folien aus Spinnenseide – Ein Hocheistungsmaterial aus der Natur in neuem Gewand
GIT Labor-Fachzeitschrift 11, 928-931
, Hess S, Lindquist S
Alternate assembly pathways of the amyloidogenic yeast prion determinant Sup35p-NM
EMBO Rep. 8,1196-1201
, Kevin D. Hermanson , Markus B. Harasim , Andreas R. Bausch
Permeability of silk microcapsules made by the interfacial adsorption of protein
Phys. Chem. Chem. Phys. 9, 6442-6446
, Römer L
The Elaborate Structure of Spider Silk: Structure and Function of a Natural High Performance Fiber
T. Scheibel (ed.): Fibrous proteins Landes Biosciences, Austin
, Vendrely C, Ackerschott C, Römer L
Molecular design of performance proteins with repetitive sequences: Recombinant flagelliform spider silk as basis for biomaterials
E. Gazit & R. Nussinov (eds): Methods in Molecular Biology. Nanostructure Design: Methods and Protocols 474, pp. 3-14
, Lammel A., Keerl D, Römer, L
Proteins: Polymers of natural origin
J. Hu, (ed.), Biomaterials: Chemistry and Physics, pp. 1-22
, Weidenauer U
Spinnenseidenproteine als pharmazeutischer Hilfsstoff
, Lin Römer
Spinnen wie die Spinnen
Nachrichten a. d. Chem. 56, 516-519
, John G.Hardy , Lin M.Römer
Polymeric materials based on silk proteins
Polymer 49, 4309-4327
, Krammer C, , Suhre MH, Kremmer E, Diemer C, Hess S, Schätzl HM, Vorberg I.
Prion protein/protein interactions: Fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells
FASEB J. 22, 762-773
, Geisler M, Pirzer T, Ackerschott C, Lud S, Garrido J, 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
, Horinek D, Serr A, Geisler M, Pirzer T, Slotta U, Lud SQ, Garrido JA, Hugel T, Netz RR.
Peptide adsorption on a hydrophobic surface results from an interplay of solvation, surface, and intrapeptide forces
Proc. Natl. Acad. Sci. USA. 105, 2842-2847
, S. Rammensee, U. Slotta, A. R. Bausch
Assembly mechanism of recombinant spider silk proteins
Proc. Natl. Acad. Sci. USA. 105, 6590-6595
, Lammel A, Schwab M, Slotta U, Winter G,
Processing conditions for spider silk microsphere formation
ChemSusChem 5, 413-416
, Slotta UK, Rammensee S, Gorb S
An engineered spider silk protein forms microspheres
Angew. Chem. Int. Edit. 47, 4592-459
, Burghard Liebmann, Daniel Hümmerich, Marcus Fehr
Formulation of poorly water-soluble substances using self-assembling spider silk protein
Colloids and Surfaces A: Physicochem. Eng. Aspects 331, 126-132
, Heim M, Keerl D,
Spider Silk: From Soluble Protein to Extraordinary Fibers
Angew. Chem. Int. Edit. 48, 2 – 15 doi: 10.1002/anie.200803341
,
Spinnenseide: Was Spiderman wissen sollte
, Römer L
The elaborate structure of spider silk: Structure and function of a natural high performance fiber
Prion 2, 154-161
, Heim M, Römer L
Hierarchical structures made of protein. The complex architecture of spider webs and their constituent silk protein
Chem. Soc. Rev. 39, 156–164 doi: 10.1039/b813273a
, , Grunwald I, Rischka K, Kast SM,
Mimicking biopolymers on a molecular scale: Nano(bio)technology based on engineered protein
Phil. Trans. Roy. Soc. London: A 367, 1727-1747 doi:10.1098/rsta.2009.0012
, Hardy JG
Production and processing of spider silk proteins
J. Polymer Sci.: Part A: Polymer Chem. 47, 3957–3963 doi: 10.1002/pola.23484
, Hardy, J.G.
Silk-inspired polymers and proteins
Biochem. Soc. Trans. 37, 677–681 doi:10.1042/BST0370677
, Andrew M. Smith
Functional amyloids used by organisms: A lesson in controlling assembly
Macromol. Chem. Phys. 210, 127-135 doi: 10.1002/macp.200900420
, Anja Hagenau Holger A. Scheidt Louise Serpell Daniel Huster Thomas Scheibe
Structural analysis of proteinaceous components in byssal threads of the mussel Mytilus galloprovincialis
Macromol. Biosciences 9, 162-168 doi: 10.1002/mabi.200800271
, Krammer C, Kryndushkin D, Suhre MH, Kremmer E, Hofmann A, Pfeifer A, Scheibel T, Wickner RB, Schätzl HM, Vorberg I.
The yeast Sup35NM domain propagates as a prion in mammalian cells
Proc. Natl. Acad. Sci. USA 106, 462-467 doi: 10.1073/pnas.0811571106
, Pirzer T, Geisler M, Hugel T.
Single molecule force measurements delineate salt, pH and surface effects on biopolymer adhesion
Physical Biol. J. 6, 025004 (8pp) doi:10.1088/1478-3975/6/2/025004
, Cyrille VézyKevin D. HermansonThomas ScheibelAndreas R. Bausch
Interfacial rheological properties of recombinant spider-silk proteins
Biointerphases 4, 43-46 doi: 10.1116/1.317493
, Suhre MH, Hess S, Golser AV
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 doi:10.1016/j.jinorgbio.2009.09.021
, Heim M, Römer L
Hierarchical structures made of protein.The complex architecture of spider webs and their constituent silk proteins
Chem. Soc. Rev. 39, 156–164 doi: 10.1039/b813273a
, Leal-Egaña A
Silk-based materials for biomedical applications
Biotechnol. Appl. Biochem. 55, 155–167 doi:10.1042/BA20090229
, Hardy, J.G.
Composite materials based on silk proteins
Progr. Polymer Sci. 35, 1093-1115 doi:10.1016/j.progpolymsci.2010.04.00
, Spiess K, Lammel A
Recombinant spider silk proteins for applications in biomaterials
Macromol. Biosciences 10 (9), 998-1007 doi: 10.1002/mabi.201000071
,
Advanced Biomaterials
Macromol. Biosciences 10, 674 doi: 10.1002/mabi.201000195
,
Spider silk from nature to bio-inspired materials
Chem Fiber Int 3, 15-16
, Heim M, Ackerschott CB
Characterization of recombinantly produced spider flagelliform silk domains
J. Struct. Biol. 170, 420–425 doi: 10.1016/j.jsb.2009.12.025
, Eisoldt L1, Hardy JG, Heim M
J. Struct. Biol. 170, 413–419 doi: 10.1016/j.jsb.2009.12.027
, Anja Hagenau
Towards the recombinant production of mussel byssal collagens
J. Adhesion 86, 10-24 doi: 10.1080/0021846090341770
, Lammel AS1, Hu X, Park SH, Kaplan DL
Controlling silk fibroin particle features for drug delivery
Biomaterials 31, 4583-4591 doi: 10.1016/j. biomaterials.2010.02.024
, Franz Hagn, Lukas Eisoldt, John G. Hardy, Charlotte Vendrely, Murray Coles
A conserved spider silk domain acts as a molecular switch that controls fibre assembly
Nature 365, 239-242 doi: 10.1038/nature08936
, David Keerl, John George Hardy
Biomimetic spinning of recombinant silk proteins
Mater. Res. Soc. Symp. Proc. 1239, VV07-20
, Kristina Spieß, Stefanie Wohlrab
Structural characterization and functionalization of engineered spider silk films
Soft Matter 6, 4168–4174 doi: 10.1039/b927267d
, , Andrew Smith
Spider Silk: Understanding the Structure–Function Relationship of a Natural Fiber
, Lukas Eisoldt, Andrew Smith
Decoding the secrets of spider silk
Materials Today 14, 80–86
, Kristina Spiess Andreas Lammel
Recombinant spider silk proteins for applications in biomaterials
Best of Macros 2011, S32-S41 doi: 10.1002/mabi.201000071
, , Andrew Smith
Recombinant spider silks – biopolymers with potential for future applications
Polymers 3, 640–661 doi:10.3390/polym3010640
, Dr. Franz Hagn, Christopher Thamm, Prof. Dr. Horst Kessler
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 doi: 10.1002/anie.201003795
, Lammel A, Schwab M, Hofer M, Winter G
Recombinant spider silk particles as drug delivery vehicles
Biomaterials 32, 2233–2240 doi: 10.1016/j.biomaterials.2010.11.060
, Anja Hagenaua, Periklis Papadopoulos, FriedrichKremer
Mussel collagen molecules with silk-like domains as load-bearing elements in distal byssal threads
J. Structural Biol. 175, 339-347 doi.org/10.1016/j.jsb.2011.05.016
, Kristin Schacht
Controlled hydrogel formation of a recombinant spider silk protein
Biomacromolecules 12, 2488–2495 doi:10.1021/bm200154k
, Kristina Spiess, Roxana Ene, Caroline D. Keenan, Jürgen Senker, Friedrich Kremerb
Impact of initial solvent on thermal stability and mechanical properties of recombinant spider silk films
J. Mater. Chem. 21, 13594-13604 doi: 10.1039/C1JM11700A
, Slotta, U., Spieß, K
Spider Silk
The Functional Fold. Useful Amyloid Structures in Nature, pp. 73-90 Pan Stanford Publishing, Singapore
, Lukas Eisoldt Christopher Thamm
The role of terminal domains during storage and assembly of spider silk proteins
Biopolymers 97, 355-361 doi: 10.1002/bip.22006
, Kai U. Claussen , Thomas Scheibel , Hans‐Werner Schmidt, Reiner Giesa
Polymer gradient materials: can nature teach us new tricks?
Macromol. Mater. Eng. 297, 938–957 doi: 10.1002/mame.201200032
, Claussen KU, Giesa R, Schmidt HW.
Learning from nature: synthesis and characterization of longitudinal polymer gradient materials inspired by mussel byssus threads
Macromol. Rapid Commun. 33, 206-211 doi: 10.1002/marc.201100620
, Bluem C
Control of drug loading and release properties of spider silk sub-microparticles
BioNanoSci. 2, 67-74 doi: 10.1007/s12668-012-0036-7
, Aldo Leal‐Egaña, Gregor Lang, Carolin Mauerer, Jasmin Wickinghoff, Michael Weber, Stefan Geimer
Interactions of fibroblasts with different morphologies made of an engineered spider silk protein
Adv. Eng. Mater. 14, B67-B75 10.1002/adem.20118007
, Keerl D
Characterization of natural and biomimetic spider silk fibers
Bioinspired, Biomimetic and Nanobiomaterials (BBN) 1, 83-94 doi: 10.1680/bbn.11.00016
, bauer F
Artificial egg stalks made of a recombinantly produced lacewing silk protein
Ang. Chemie Intl. Edit. 124, 6627-6630 doi: 10.1002/anie.201200591
, Aldo Leal-Egañaa
Interactions of cells with silk surfaces
J. Mater. Chem. 22, 14330-14336 doi: 10.1039/c2jm31174g
, , Stefanie Wohlrab, Susanne Müller, Stefanie Neubauer,Horst Kessler, Aldo Leal-Egaña
Cell adhesion and proliferation on RGD-modified recombinant spider silk proteins
Biomaterials 33, 6650-6659 doi: 10.1016/j.biomaterials.2012.05.069
, Seth L. Young, Maneesh Gupta, Christoph Hanske, Andreas Fery, Vladimir V. Tsukruk
Utilizing conformational changes for patterning thin films of recombinant spider silk proteins
Biomacromolecules 13, 3189-3199 doi: 10.1021/bm300964h
, Stefanie Wohlrab, Kristina Spießa
Varying surface hydrophobicities of coatings made of recombinant spider silk proteins
J. Mater. Chem. 22, 22050-22054 doi: 10.1039/c2jm35075k
, Bauer F, Bertinetti L, Masic A,
Dependence of mechanical properties of lacewing egg stalks on relative humidity
Biomacromolecules. 13, 3730-3735 doi: 10.1021/bm301199d
, Andrew Smith
Hierarchical Protein Assemblies as a Basis for Materials
Architecture, pp. 256-281 RCS Publishing, Cambridge. doi: 10.1039/9781849737555-00256
, Lauterbach A.Y.,
Determining the Environmental Benefit of Artificial Spider Silk Products
CTSI-Cleantech 2013, 108-111 ISBN: 978-1-4822-0586-2
, Stefanie Wohlrab, Christopher Thamm
The Power of Recombinant Spider Silk Proteins
doi: 10.1007/978-94-007-7119-210
, AnielaHeidebrecht
Recombinant Production of Spider Silk Proteins
Adv. Appl. Microbiol. 82, 115-153 doi: 10.1016/B978-0-12-407679-2.00004-1
, Eileen S. Lintz
Dragline, egg stalk, and byssus – A comparison of outstanding protein fibers
Adv. Funct. Mater. 23, 4467–4482 doi: 10.1002/adfm.201300589
,
Spinnenseide – Biotechfaser mit naturidentischer Belastbarkeit
Chemie & More, 4, 3-5
, Hofmann JP, Denner P, Nussbaum-Krammer C , Kuhn PH, Suhre MH, Lichtenthaler SF, Schätzl HM, Bano D, Vorberg IM.
Cell-to-cell propagation of infectious cytosolic protein aggregates
PNAS 110, 5951–5956 doi: 10.1073/pnas.1217321110
, Gregor Lang, S Jockish
Air filter devices including nonwoven meshes of electrospun recombinant spider silk proteins
J. Vis. Exp. 75, e50492 (link) doi: 10.3791/50492
, Claussen KU, Lintz ES, Giesa R, Schmidt HW
Protein gradient films of fibroin and gelatine
Macromol. BioSci. 13, 1396–1403 doi: 10.1002/mabi.201300221
, John G. Hardy, Aldo Leal‐Egaña
Engineered spider silk protein-based composites for drug delivery
Macromol. BioSci. 13, 1431–1437 doi: 10.1002/mabi.201300233
, Martin P. Neubauer, Claudia Blüm,Elisa Agostini, Julia Engert, Andreas Fery
Micromechanical characterization of spider silk particles
Biomater. Sci. 1, 1160-1165 doi: 10.1039/C3BM60108K
, Nicolas Helfricht, Maria Klug, Andreas Mark,Volodymyr Kuznetsov, Claudia Blüm,Georg Papastavrou
Surface properties of spider silk particles in solution
Biomater. Sci. 1, 1166-1171 doi: 10.1039/C3BM60109A
, Felix Bauer, Stefanie Wohlrab
Controllable cell adhesion, growth and orientation on layered silk protein films
Biomater. Sci. 1, 1244-1249 doi: 10.1039/c3bm60114e
, Claudia Blüm, Alfons Nichtl
Spider silk capsules as protective reaction containers for enzymes
Adv. Funct. Mater. 24, 763–768 doi: 10.1002/adfm.201302100
, Heim M, Elsner MB
Lipid-specific ß-sheet formation in a mussel byssus protein domain
Biomacromolecules 14, 3238-45 doi: 10.1021/bm400860y
, David Keerl
Rheological characterization of silk solutions
Green Materials 2, 11 –23 doi: 10.1680/gmat.13.00009
, Neuenfeldt M,
Silks From Insects – From Natural Diversity to Application
In: K. H. Hoffmann (ed): Insect Molecular Biology and Ecology. CRC Press ISBN 9781482231885
,
Die Natur als Vorbild für bioinspirierte Materialien der Zukunft
, Anja Hagenau, Michael H.Suhre
Nature as a blueprint for polymer material concepts: protein fiber-reinforced composits as holdfasts of mussels
Progr. Polym. Sci. 39, 1564-1583 doi: 10.1016/j.progpolymsci.2014.02.007
, Schacht K
Processing of recombinant spider silk proteins into tailor-made materials for biomaterials applications
Curr. Opin. Biotechnol. 29, 62-69 doi: 10.1016/j.copbio.2014.02.015
, Dr. Gregor Lang
Multifunktionale Spinnenseide – ein vielversprechender Werkstoff
MaschinenMarkt 26, 36-39
, Christian B. Borkner†, Martina B. Elsner
Coatings and films made of silk proteins
ACS Appl. Mater. Interface. 29, 62-69 doi: 10.1021/am5008479
, Cordt Zollfrank,Heike Seitz, Nahum Travitzky
Bioinspired materials engineering
Ullmann’s Encyclopedia of Industrial Chemistry doi: 10.1002/14356007.s04_s01
, ,
Self-assembly of nucleic acids, silk and hybrid materials thereof
J. Phys. Condens. Matter 26, 503102 doi: 10.1088/0953-8984/26/50/503102
, Heidebrecht A
Spionik – Biotech Spinnenseide und ihre Einsatzgebiete
GIT Bioforum 2, 20-22
, ,
Nanomaterial building blocks based on spider silk–oligonucleotide conjugates
ACS Nano 8, 1342-1349 doi: 10.1021/nn404916f
, Suhre MH, Gertz M, Steegborn C
Structural and functional features of a collagen-binding matrix protein from the mussel byssus
Nat. Comm., 5, 3392 doi: 10.1038/ncomms4392
, Suhre MH, Gertz M, Steegborn C,
Structural and functional features of a collagen-binding matrix protein from the mussel byssus
J. Struct. Biol. 186, 75-85 doi: 10.1016/j.jsb.2014.02.013
, Hardy JG, Pfaff A, Leal-Egaña A, Müller AH,
Glycopolymer functionalization of engineered spider silk protein based materials for improved cell adhesion
Macromol. Biosci., 14, 936-42 doi: 10.1002/mabi.201400020
, Michael H. Suhre, Clemens Steegborn, Melanie Gertzb
Crystallization and preliminary X-ray diffraction analysis os PTMP1
Acta Crystallographica Section F 70, 769-772 doi: 10.1107/S2053230X14006165
, , Magdeburg M
Influence of repeat numbers on self-assembly rates of repetitive recombinant spider silk proteins
J. Struct. Biol., 186, 431-437 doi: 10.1016/j.jsb.2014.03.010
, , Markus Drechsler
Controlled hierarchical assembly ofspider silk-DNA chimeras into ribbons and raft-like morphologies
Nano Lett.., 14, 3999−4004 doi: 10.1021/nl501412k
, Anja Yvonne Lauterbach
Life cycle assessment of spider silk nonwoven meshes in an air filtration device
Green Materials., 3: 15-24 doi: 10.1680/gmat.14.00011
, R. H. Zeplin, A.-K. Berninger, N. C. Maksimovikj, P. van Gelder, H. Walles
Verbesserung der Biokompatibilität von Silikonimplantaten
Handchir. Mikrochir. Plast. Chir., 46: 336-41 doi: 10.1055/s-0034-1395558
,
Engineering of rec SSP allows defined drug uptake and release
TechConnect Briefs 2015: Biotech, Biomaterials and Biomedical CRC Press
, Doblhofe E, Heidebrecht A,
To spin or not to spin: spider silk fibers and more
Appl. Microbiol. Biotechnol. 99: 9361-9380 doi: 10.1007/s00253-015-6948-8
, Tomasz Jungst, Willi Smolan, Kristin Schacht, Jürgen Groll
Strategies and molecular design criteria for 3D printable hydrogels
Chem. Rev.. 99: 9361-9380 doi: 10.1021/acs.chemrev.5b00303
,
Vom Spinnennetz zur High-Tech-Faser
Naturwiss. Rundschau.. 68: 524-525
, Doblhofer E
Engineering of recombinant spider silk proteins allows defined uptake and release of substances
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