Amyloidogenic Peptide Fragments Designed From Bacterial Collagen-like Proteins Form Hydrogel

DOI zum Zitieren der Version auf EPub Bayreuth: https://doi.org/10.15495/EPub_UBT_00009530
URN to cite this document: urn:nbn:de:bvb:703-epub-9530-8

Title data

Sagar, Vamika ; Ng, Xuen J. ; Lechel, Lukas ; Rajwar, Ashish Chand ; Bargel, Hendrik ; Jalan, Abhishek A.:
Amyloidogenic Peptide Fragments Designed From Bacterial Collagen-like Proteins Form Hydrogel.
In: Advanced Functional Materials. Vol. 36 (2026) Issue 40 . - e32055.
ISSN 1616-3028
DOI der Verlagsversion: https://doi.org/10.1002/adfm.202532055

	Format: PDF Name: Adv Funct Materials - 2026 - Sagar - Amyloidogenic Peptide Fragments Designed From Bacterial Collagen‐like Proteins Form.pdf Version: Published Version Available under License Creative Commons BY 4.0: Attribution
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Project information

Project title:	Project's official title Project's id TRR 225: Von den Grundlagen der Biofabrikation zu funktionalen Gewebemodellen 326998133 Open Access Publizieren No information
Project financing:	Deutsche Forschungsgemeinschaft

Abstract

Bacterial collagen-like proteins (CLPs) are composed of tandem Gly-X-Y sequence repeats, but, unlike metazoan collagens, their X- and Y-positions are enriched in hydrophobic and polar residues rather than proline. This distinctive sequence bias suggests that CLPs may harbor sequence features that could promote amyloid-like assembly. Using bioinformatic screening of CLPs, we identified amyloidogenic motifs enriched in alanine, isoleucine, leucine, or valine at the X-position and threonine at the Y-position. Guided by these findings, we designed a focused library of peptides incorporating Gly-X-Thr triplet and the highly abundant GATGVT sextet repeats. Peptides containing Gly-X-Thr produced insoluble fibers, restricting exploration of material properties. In contrast, peptides containing GATGVT repeats formed micrometer-long fibers that physically crosslinked into a robust hydrogel upon centrifugation. Circular dichroism (CD) and Fourier Transform Infrared Spectroscopy (FTIR) revealed length-dependent variations in secondary structure. Imaging of the higher-order structures confirmed densely packed fiber networks while rheological measurements indicated sequence-length-dependent viscoelastic behavior. Notably, a 30 residue GATGVT peptide hydrogel supported high in vitro cell viability of fibroblasts. Overall, these findings suggest that CLPs are an underexplored reservoir of sequence motifs with promising biomaterial potential.

Further data

Item Type:	Article in a journal
DDC Subjects:	600 Technology, medicine, applied sciences > 620 Engineering
Institutions of the University:	Faculties > Faculty of Engineering Science > Chair Biomaterials Faculties Faculties > Faculty of Engineering Science
Language:	English
Originates at UBT:	Yes
URN:	urn:nbn:de:bvb:703-epub-9530-8
Date Deposited:	28 Jul 2026 10:55
Last Modified:	28 Jul 2026 10:56
URI:	https://epub.uni-bayreuth.de/id/eprint/9530

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