# Spontaneous Crimping of Gelatin Methacryloyl Nanofibrils Induced by Limited Hydration

**Authors:** Chien-Wei Wu, Tzu-Yin Huang, Liang-Jie Huang, Yi-Wei Kuo, Chin-Lin Guo, Po-Ling Kuo

PMC · DOI: 10.1021/acsbiomaterials.5c00828 · 2025-07-18

## TL;DR

Researchers developed a method to create crimped nanofibrils that mimic natural collagen, improving cell behavior and offering new tools for tissue engineering.

## Contribution

A novel method to induce spontaneous, tunable crimping in gelatin methacryloyl nanofibrils using limited hydration.

## Key findings

- Crimped nanofibrils matched the size and crimping of native collagen fibrils.
- Crimping reduced network stiffness but increased stretchability, similar to native tissues.
- Crimped fibrils promoted cell translocation and altered fibroblast protein expression.

## Abstract

The crimped appearance of native collagen fibrils in
youthful tissues
serves as a mechanical buffer and phenotype determinant for resident
cells. In vitro platforms emulating these native
crimped networks facilitate the study of cell-matrix dynamics in various
pathophysiological contexts. However, creating fibrillar networks
with sizes and crimping matching native tissues using collagen-derived
substrates remains challenging. We present an innovative approach
to produce spontaneous, tunable crimping of electrospun, aligned gelatin
methacryloyl nanofibrils using limited hydration. The diameter of
the synthesized fibrils approximated that of native fibrils. Beyond
individual fibril crimping, the network exhibited large-scale, periodic
crimping with wavelengths matching native collagen networks. Tensile
stress tests revealed that crimping reduced network stiffness but
enhanced stretchability, consistent with native tissues. Additionally,
crimping promoted cell translocation into the network. Fibroblasts
cultured on crimped fibrils showed smaller cell areas, higher vinculin
and α-tubulin expression, and lower α-smooth muscle actin
levels compared to those on straight fibrils. This novel method not
only replicates the native fibril characteristics using collagen-derived
materials, but also offers a valuable tool for advancing our understanding
of cell-matrix interactions, with significant implications for tissue
engineering and regenerative medicine.

## Linked entities

- **Proteins:** LOC110462068 (vinculin-like), LOC126710533 (tubulin alpha chain-like)

## Full-text entities

- **Genes:** TUBA1B (tubulin alpha 1b) [NCBI Gene 10376] {aka K-ALPHA-1}, VCL (vinculin) [NCBI Gene 7414] {aka CMD1W, CMH15, HEL114, MV, MVCL, VINC}

## Figures

12 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12344688/full.md

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Source: https://tomesphere.com/paper/PMC12344688