Dr. Humenik, Martin

Open Resume

Hybrid Materials

Research Overview

Self-assembly as a design principle

Self-assembly operates through autonomous, non-covalent interactions between molecular building blocks. It requires no external energy input and imposes no fundamental limit on dimensional scaling — from the nanometer to the macroscopic. Nature exploits this logic to produce materials of exceptional organisation and function: bone, mollusc shell, spider silk.

 

Our group applies these principles to engineer hybrid biomaterials that combine the programmability of nucleic acid nanotechnology with the structural robustness of recombinant spider silk proteins. The result is a versatile platform for spatially defined, biologically active nanomaterials that can interface with cells, enzymes, and synthetic nanostructures.

 

Hybrid Biomaterials · Self-Assembly · Nanotechnology

 

Research Pillars

I.

DNA–Protein Conjugate Chemistry

Site-specific azide–alkyne “click” coupling links recombinant eADF4(C16) spider silk to designer oligonucleotides. We study how chemical conjugation changes fibril morphology, kinetics of self-assembly, and surface reactivity.

II.

Programmable Hierarchical Assembly

DNA hybridisation directs the spatial organisation of silk moieties in solution, yielding branched structures, ribbons and micro-rafts governed by designed complementarity and temperature gradients.

 

III.

Micropatterned Nanohydrogels

Photolithography and micro-contact printing define where silk fibrils nucleate and grow on a surface. The resulting fibrous networks swell and soften like hydrogels, creating three-dimensional niches within arbitrary microstructures.

IV.

Aptameric Surface Functionalisation

DNA aptamers conjugated to silk nanohydrogels confer bioselective binding capacity — enabling specific capture of proteins, enzymes, growth factors and living cells without compromising fibrillar scaffold integrity.

 

Applications and Perspective

A multifunctional platform for biology and medicine

The combination of spider silk’s mechanical resilience and environmental stability with the programmability of nucleic acid interactions creates a uniquely versatile scaffold. Below are the application domains our technology is positioned to address.

🔬

Circulating tumour cell isolation

Aptamer-functionalised nanohydrogel microarrays selectively capture specific cancer cell types from complex biological fluids. Low non-specific binding of the silk scaffold minimises background, improving sensitivity for liquid biopsy applications.

💊

Controlled drug and protein delivery

Aptamer-gated silk nanohydrogels release therapeutic proteins in response to molecular triggers. Redox- and pH-sensitive silk-based drug carriers (published in Biomacromolecules 2020) extend this to small-molecule drugs, enabling stimuli-responsive implantable depots.

🧫

Programmable tissue engineering scaffolds

DNA-directed cell patterning on three-dimensional nanohydrogel microstructures provides spatially defined niches for tissue formation. Multicomponent systems with co-immobilised growth factors guide stem cell differentiation and organ-on-chip construction.

🧬

Biosensors and diagnostics

Silk–DNA hybrids functionalised with enzyme reporters or gold nanoparticles form the basis for highly sensitive electrochemical and optical biosensors, building on our group’s foundational work in esterase-dendrimer electrochemical detection.

🦠

Anti-fouling implant coatings

eADF4(C16) nanofibrillar silk coatings do not support bacterial adhesion and repel microbobes, while they allow specific mammalian cell binding — making them strong candidates for next-generation infection-resistant bioselective implant surfaces.

⚗️

Regenerative medicine

Fibrillar nanohydrogel networks including cell-adhesion motifs and signalling factors provide tunable microenvironments for tissue regeneration. Integration with photolithographic micropatterning enables spatially graded scaffolds matching native tissue architecture.

 

Recent Research Highlights

Surface Science · 2025

Nanostructured protein coatings with tunable cell affinity

A comprehensive review co-authored by Humenik and Scheibel maps the design space of recombinant spidroin-based nanostructured surface coatings. Bioengineered spidroin variants now enable surfaces with programmable affinity — from cell-repellent nanohydrogel coatings that resist bacterial fouling to aptamer-functionalised layers that capture specific cancer cell types on demand.

Humenik & Scheibel, Advanced Materials 2025, 37.

Cancer Diagnostics · 2022

Aptamer-modified nanohydrogel microarrays for cancer cell capture

Photolithography combined with spider silk self-assembly produces cell-repellent micropatterned nanofibrillar networks. Incorporation of DNA aptamers targeting PTK7 receptor-positive cancer cells (HeLa) enables bioselective, reversible immobilisation — a foundation for circulating tumour cell isolation and on-chip diagnostics.

Lamberger, Bargel & Humenik, Advanced Functional Materials 2022, 32.

 

Cell Patterning · 2022

DNA-guided cell attachment and patterning on nanohydrogels

Spider silk nanohydrogels functionalised with defined DNA sequences direct specific cell attachment and spatial patterning. Pre-programmed DNA–cell interactions allow arbitrary positioning of living cells on the scaffold surface — advancing programmable tissue architectures.

Heinritz, Lamberger, Kocourková, Minařík & Humenik, ACS Nano 2022, 16.

Self-Assembly Kinetics · 2023

Secondary nucleation drives spider silk fibril growth

Global kinetic analysis reveals that recombinant spider silk fibril formation proceeds via secondary nucleation — a mechanistic insight with direct implications for controlling gelation rates, fibril dimensions, and material homogeneity in processing applications.

Hovanová, Hovan, Žoldák, Sedlák & Humenik, Protein Science 2023, 32.

 

Protein Release · 2020

Aptamer-gated protein binding and controlled release

Anti-thrombin aptamers chemically conjugated to eADF4(C16) nanohydrogels enable bio-selective protein capture and stimulus-triggered release. This modular approach extends to growth factors and enzymes, opening routes to implantable delivery devices.

Humenik, Preiß, Gödrich, Papastavrou & Scheibel, Materials Today Bio 2020, 6.

Antibody Engineering · 2026

Directed antibody functionalization

Incorporation of non-canonical amino acids into recombinant silk proteins enables site-directed conjugation of antibodies to nonwoven silk membranes — providing oriented, fully active antibody display for biosensor and immunodiagnostic applications.

Lacombe, Leonhardt, Humenik, Wiltschi & Scheibel, Advanced Materials 2026, 38.

Research Projects

Schiller, Tim

tim.schiller(at)uni-bayreuth.de

0921 55 6711

Implementation of Nanohydrogels in Biosensors (TiS)

 

Recombinant spider silk proteins self-assemble into β-sheet-rich fibrils under mild aqueous conditions, a process that is controlled by phosphate ions. This nucleation mechanism enables also the formation of protein nanohydrogels – immobilized, interconnected networks that exhibit swelling behavior.

Catalytically active proteins (enzymes) require precise environmental conditions to preserve their activity, particularly when immobilized. Spider silk-based nanohydrogels allow for the diverse covalent or non-covalent incorporation of enzymes, providing a tunable protective microenvironment. Furthermore, the nanohydrogels can be transferred onto various surfaces, including gold electrodes and electrospun nonwovens, offering potential applications in biosensors.

Prinzler, Miriam

miriam1.prinzler(.at.)uni-bayreuth.de

0921 55 6711

Nanohydrogel Modifications for TE (MP)

 

The targeted modification of biomaterial surfaces enables the development of systems for applications in the field of tissue engineering. Through functionalization with DNA aptamers, biomaterials can be engineered to bind specific target molecules with high affinity and selectivity. The goal is to develop multifunctional biomaterials that specifically influence cellular processes and support tissue regeneration.

 

Project 1: Chemical Functionalization of Biomaterials

Various biomaterial platforms, such as chitosan-based materials, recombinant spider silk materials, and fiber-based PCL scaffolds, are chemically modified for the immobilization of aptamers. Suitable coupling strategies are tested to stably bind aptamers to the materials and preserve their functionality.

 

Project 2: Binding and Release of Bioactive Molecules

Through the immobilization of specific aptamers, biomaterials are designed to specifically bind, store, and controllably release growth factors and other signaling molecules. The study investigates how surface modification influences binding and release properties.

 

Project 3: Cell-Biomaterial Interactions

Biomaterials functionalized with aptamers are being investigated for their interactions with cells. The focus is on effects on cell adhesion, proliferation, and differentiation in order to evaluate the materials’ potential for applications in tissue engineering.

Best, Nadine

nadine.best(.at.)uni-bayreuth.de

0921 55 6710

Characterization of physicochemical properties of nanohydrogels for biomedical applications

 

The recombinant spider silk protein eADF4(C16) can self-assemble into β-sheet-rich protein fibrils and their formation is triggered by phosphate ions. This mechanism serves as a blueprint for the fabrication of nanometer-thin, immobilized hydrogels that have already shown promise in biomedical applications.

Project 1: Characterization of spider silk-based nanohydrogels

The structure and function of the nanometer-sized nanohydrogels has not yet been thoroughly characterized or understood. For this reason, my project aims to characterize the physicochemical properties of nanohydrogels focusing on, for example, swelling behavior, nanomechanics, self-healing and interaction with other proteins. The understanding of the function-properties relation enables tailored applications of nanohydrogels.

Project 2: Aptamer-functionalized nanohydrogels for cell patterning

Nanohydrogels can be modified with DNA strands via click chemistry. In this project, I will utilize photo-click chemistry to attach different aptamers to nanohydrogels in defined patterns, enabling the subsequent binding of different cell types to the surface in distinct spatial arrangements. The patterned, immobilized cells are intended to resemble a two-dimensional model that mimics the composition of artificial tissue.

Project 3: DNA origami–nanohydrogel depots for controlled drug release

DNA origami structures have emerged as promising drug carriers, as anticancer agents can be incorporated into their DNA framework for targeted delivery into cancer cells. This project focuses on the development of DNA-modified nanohydrogels that function as a DNA origami drug depot and reliably releases the retained DNA origami structures. This system can potentially be employed in cancer treatments, for example, in ocular oncology.

Publications

Humenik M. & Scheibel T.

Nanostructured protein surfaces inspired by spider silk

Adv. Mater. 2025, e08959

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. 2020, 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 2020, 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

Scheibel T., Trossmann V.T., Lechner A., Bargel H., Humenik M. & Žurovec M.

Bioinspirierte Klebstoffe zur Anwendung in wässrigen Flüssigkeiten

Adhaes. Kleb. Dicht. 2022, 66, 34–39

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

Processing of continuous non-crosslinked collagen fibers for microtissue formation at the muscle-tendon interface

Adv. Funct. Materials, 2022, 32, 2112238

Laomeephol C., Vasuratna A., Ratanavaraporn J., Kanokpanont S., Luckanagul J., Humenik M., Scheibel T. & 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, 2021, 112, e23412

Lefevre M., Flammang P., Aranko A.S., Linder M.B., Scheibel T., Humenik M, Leclercq M. , Surin M., Tafforeau L,, Wattiez R., Leclère P. & Hennebert E.

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

Acta Biomaterialia, 112 (2020), 62-74

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, (2020), 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, (Adv. 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, 2019, 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

WIREs Nanomed. Nanobiotechnol., 2018, 10: e1509  

Molina A., Humenik M. & Scheibel T.

Nanoscale patterning of surfaces via DNA directed spider silk assembly

Biomacromol., 2019, 20, 347-352

Humenik M., Mohrand M. & Scheibel T.

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

Bioconjugate Chem., 2018, 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., 2018, 28, 1800216

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