Hydrogels Formed by the Self‐Assembly of Collagen‐Mimetic Peptides With a Constrained Backbone Structure

Self-assembling peptides have attracted increasing attention as building blocks for developing functional materials. Among them, collagen-mimetic peptides (CMPs) represent a class of self-assembling systems. However, although short-chain CMPs spontaneously fold into thermodynamically stable triple-helical trimers, they fail to further undergo supramolecular assembly to form hydrogels. We report a new strategy for supramolecular hydrogel formation based on CMPs. The designed peptide, termed kinkCMP, features a kinked backbone introduced at the center of the sequence via adjacent disulfide bonds. The kinkCMP forms a gel, and its gel denaturation temperature can be tuned by varying the peptide chain length. Moreover, the hydrogel can be used as a cell culture scaffold. These results provide a versatile approach for constructing supramolecular hydrogels based on CMPs, expanding the design strategies for peptide-based functional materials.

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Publication Details

Journal
Chemistry - A European Journal
Published
2026-01-07
DOI
https://doi.org/10.1002/chem.202503278
Primary Topic
Collagen: Extraction and Characterization
Type
article
Field-Weighted Citation Impact
0.00

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article

Hydrogels Formed by the Self‐Assembly of Collagen‐Mimetic Peptides With a Constrained Backbone Structure

Kazunori K. Fujii, M Noto, Takaki Koide, T Hiroi et al.
Chemistry - A European Journal
Collagen: Extraction and Characterization
article

Hydrogels Formed by the Self‐Assembly of Collagen‐Mimetic Peptides With a Constrained Backbone Structure

Kazunori K. Fujii, M Noto, Takaki Koide, T Hiroi, Yuetsu Shu
article en

Abstract

Self-assembling peptides have attracted increasing attention as building blocks for developing functional materials. Among them, collagen-mimetic peptides (CMPs) represent a class of self-assembling systems. However, although short-chain CMPs spontaneously fold into thermodynamically stable triple-helical trimers, they fail to further undergo supramolecular assembly to form hydrogels. We report a new strategy for supramolecular hydrogel formation based on CMPs. The designed peptide, termed kinkCMP, features a kinked backbone introduced at the center of the sequence via adjacent disulfide bonds. The kinkCMP forms a gel, and its gel denaturation temperature can be tuned by varying the peptide chain length. Moreover, the hydrogel can be used as a cell culture scaffold. These results provide a versatile approach for constructing supramolecular hydrogels based on CMPs, expanding the design strategies for peptide-based functional materials.

Chemistry - A European JournalVol. 32(10)
Waseda University (JP)
Waseda University
Openalex Percentile: Top 94%
Collagen: Extraction and Characterization
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