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Nanostructured Protein Surfaces Inspired by Spider Silk

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Humenik, Martin ; Scheibel, Thomas:
Nanostructured Protein Surfaces Inspired by Spider Silk.
In: Advanced Materials. Bd. 37 (2025) Heft 51 . - e08959.
ISSN 1521-4095
DOI: https://doi.org/10.1002/adma.202508959

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Abstract

Spider silk is renowned for its exceptional mechanical properties, surpassing those of many natural and synthetic materials. This review focuses on biotechnologically produced recombinant spidroin variants inspired by well-understood major ampullate spider silk proteins (=spidroins), which are role models for understanding molecular composition, architecture, and the nanoscopic and mesoscopic structures formed through self-assembly and phase separation of spider silk fibers. The use of recombinant spidroins is explored to fabricate functionalized nanostructured surfaces, and molecular engineering is highlighted to tailor the interfacial properties of various morphologies, including particles, capsules, electrospun nanofibers, films/coatings, macroscopic nanofibril-based hydrogels, and nanohydrogel coatings. One focus is on functionalization of spidroins with peptide tags enabling a variety of affinity-based targets from cellular markers to inorganic nanoparticles, and allowing for instance specific drug delivery, cell accommodation in hydrogels, or bioselective immobilization of cells on surfaces. Furthermore, applying nanostructured spidroin coatings in combination with photo- and soft-lithography techniques is demonstrated, which can be used to produce micro- and nanostructured patterns exhibiting confined, spidroin-defined targeting, affinity, or repulsion properties.

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Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: coatings; functional materials; hydrogels; particles; self-assembly; spinning
Institutionen der Universität: Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien > Lehrstuhl Biomaterialien - Univ.-Prof. Dr. Thomas Scheibel
Forschungseinrichtungen > Zentrale wissenschaftliche Einrichtungen > Bayreuther Zentrum für Kolloide und Grenzflächen - BZKG
Forschungseinrichtungen > Zentrale wissenschaftliche Einrichtungen > Bayreuther Zentrum für Molekulare Biowissenschaften - BZMB
Forschungseinrichtungen > Zentrale wissenschaftliche Einrichtungen > Bayreuther Materialzentrum - BayMAT
Forschungseinrichtungen > Institute in Verbindung mit der Universität > Bayerisches Polymerinstitut (BPI)
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften
Eingestellt am: 04 Feb 2026 13:07
Letzte Änderung: 04 Feb 2026 13:07
URI: https://eref.uni-bayreuth.de/id/eprint/96004