Dr. Humenik, Martin

Open Resume

Hybrid Materials

Self-assembly is based on autonomous mechanism of non-covalent interactions between distinct building blocks. Related processes do not require external energy source and have no limitation in dimensional scaling. Such “bottom up” formation structures at different hierarchical levels is inspired by natural processes, which enable highly organized materials with exceptions properties such as bones, shells or spider silks.

Application of the self-assembly principles to control nano- and micro scaled structuring of biomaterials is in focus of our group.

Research Projects

Dr. Humenik, Martin


0921-55 6725

DNA-Protein Hybrids

Nucleic acids could self-assemble into many different nano-structures with precision and predictability, which is unrivaled among the natural and synthetic materials. One of the best example for such high fidelity is represented by the DNA origami programming and folding. On the other hand, recombinant fibrous proteins also self-assemble into nanofibrils, supramolecular structures of densely packed cross-ß sheets. Such fibrils, typically 10 nm in diameter and hundreds of nanometers long, possess high physico-chemical stability as well as mechanical rigidity. Such systems represent attractive scaffolds for the generation of ordered nanomaterials.

To take advantage of both protein and DNA materials, we chemically combine recombinant spider silk proteins and nucleic acids in hybrid entities. Their fundamental properties are investigated to realize their utilization in materials research. One focus is the  study of new chemical modifications and conjugations of the building blocks, arrangements protein moieties upon hybridizations of DNA, corresponding morphology and structure of conjugate fibrils. Further, we use specific DNA hybridization to trigger nucleation of the fibrils into hierarchical structures on surfaces. We combine soft- and photolithography techniques with the DNA hybrids to spatially define self-assembly of the supramolecular structures in 2D and 3D. Our technology enables formation of fibrillar nanohydrogel-like networks within arbitrary shaped microstructructures. Employing chemically coupled DNA aptameric functionalities, we can bind enzymes, growth factors or even whole cells specifically.

Fig. 1: Self-organization of DNA-protein hybrid materials in bottom up manner in solutions: Spider silk moieties in the hybrids, prepared by a chemical conjugation with DNA, were spatially arranged into branched structures using designed DNA hybridization and self-assembled into ribbons, which further self-organized into micro-rafts due to DNA interaction at specific temperature gradients.


Fig. 2: Pattering of the hybrid materials using DNA-directed hybridization technology: Surfaces modified by capture DNA were specifically linked to complementary DNA-spider silk conjugates on defined position using micro-contact printing technology. Immobilized conjugates served as nucleation sides for silk fibrils growth from the surface.


Fig. 3: Microstructured nanohydrogels. a) photolithography processed positive-tone photoresist with micro-wells for spatially defined protein self-assembly on the surface; b) AFM scans of the self-assembled fibrous microstructures after photoresist removal; c) immobilized fibrous networks reveal nano hydrogel properties like swelling and softening on the surface; d) cells specifically immobilized on the DNA-modified spider silk microstructures via pre-defined DNA-cell interaction.



Taken together, processing or structuring spider silk proteins and bio-functionalized hybrids thereof into nanohydrogel-based platform allows integrating different functionaries into immobilized fibril networks. Exploiting such biomolecular tools, more complex patterns consisting of multiple, unique functionalities, such as conjugated enzymes, aptamers or gold nanoparticles, deposited in 1D along the growing fibrils and in 2D pattern on surfaces are likely feasible. Concomitant possibility for specific immobilization of living cells as well as programmable nanohydrogel patterning offer a platform with great potential for development of numerous biological and biomedical applications in regenerative medicine and cell separations and analytics.


Fig. 4: Universal platform of spider silk nanofibrillar scaffold for multifunctional surface modifications


M. Humenik

Publication list PD Dr. Martin Humenik

See Google Scholar for full publication list

Kocourkova K., Musilova L., Smolka P., Mracek A., Humenik M., Minarik A.

Factors determining self-assembly of hyaluronan

Carbohydr. Polym. 254, 117307

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

Wang Y., Stanzel M., Gumbrecht W., Humenik M., Sprinzl M.

Esterase 2-oligodeoxynucleotide conjugates as sensitive reporter for electrochemical detection of nucleic acid hybridization

Biosens.Bioelectron. 22, 1798-1806

Humenik M., Huang Y., Wang Y., Sprinzl M.

C-terminal incorporation of bio-orthogonal azide groups into a protein and preparation of protein-oligodeoxynucleotide conjugates by Cu(l)-catalyzed cycloaddition

ChemBioChem 8, 1103-1106

Humenik M., Poehlmann C., Wang Y., Sprinzl M.

Enhancement of Electrochemical Signal on Gold Electrodes by Polyvalent Esterase-Dendrimer Clusters

Bioconjug.Chem. 19, 2456-2461

Minarik A., Humenik M., Li S., Huang Y., Krausch G., Sprinzl M.

Ligand-Directed Immobilization of Proteins through an Esterase 2 Fusion Tag Studied by Atomic Force Microscopy

ChemBioChem 9, 124-130

Poehlmann C., Humenik M., Sprinzl M.

Detection of bacterial 16S rRNA using multivalent dendrimer-reporter enzyme conjugates

Biosens.Bioelectron. 24, 3383-3386

Poehlmann C., Wang Y., Humenik M., Heidenreich B., Gareis M., Sprinzl M.

Rapid, specific and sensitive electrochemical detection of foodborne bacteria

Biosens. Bioelectron. 24, 2766-2771

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

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

Impacts of Blended Bombyx mori Silk Fibroin and Recombinant Spider Silk Fibroin Hydrogels on Cell Growth

Polymers. 2021, 13, 4182

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

Patterning of protein-based materials

Biopolymers, 2020; online Dec. 2020

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

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

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

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

Aqueous electrospinning of recombinant spider silk proteins

Mater. Sci. Eng. C, 106, 110145

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.

Humenik M., Smith A., Scheibel T.

Recombinant spider silks – biopolymers with potential for future applications

Polymers 3, 640–661  

Humenik M., Scheibel T.

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

J. Phys. Condens. Matter 26, 503102

Humenik M., Scheibel T.

Nanomaterial building blocks based on spider silk–oligonucleotide conjugates

ACS Nano 8, 1342-1349

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

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

Ion and seed dependent fibril assembly of a spidroin core domain

J. Struct. Biol. 191: 130–138

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., Lang G., Scheibel T.

Silk nanofibril self-assembly versus electrospinning

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

Molina A., Humenik M, Scheibel T.

Nanoscale patterning of surfaces via DNA directed spider silk assembly

Biomacromol., 20, 347-352

Humenik M., Mohrand M., Scheibel T.

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

Bioconjugate Chem., 29: 898 – 904.

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

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