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

## TL;DR

Researchers designed kinked collagen-like peptides that self-assemble into tunable hydrogels, which can be used as cell culture scaffolds.

## Contribution

A new strategy for supramolecular hydrogel formation using kinked collagen-mimetic peptides with tunable thermal stability.

## Key findings

- KinkCMPs form hydrogels with denaturation temperatures that can be adjusted by varying the peptide chain length.
- The hydrogels are suitable for use as cell culture scaffolds.
- The kinked backbone structure promotes supramolecular assembly.

## 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.

Kinked collagen‐mimetic peptides (kinkCMPs), whose backbone is constrained by a disulfide bond, are designed to induce hydrogel formation. The kinked backbone promotes supramolecular assembly into tunable hydrogels with thermal stability depending on length. The resulting gels are also applicable as cell culture scaffolds, providing a new strategy for peptide‐based biomaterials.