Review Article | Open Access
Volume 2025 |Article ID 100004 | https://doi.org/10.1016/j.bidere.2025.100004

Protein-based materials: Applications, modification and molecular design

Alitenai Tunuhe,1,3 Ze Zheng,1,3 Xinran Rao,1 Hongbo Yu,1 Fuying Ma,1 Yaxian Zhou ,2 and Shangxian Xie 1

1Department of Biotechnology, Key Laboratory of Molecular Biophysics of MOE, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, 430074, China
2Guangxi Shenguan Collagen Technology Research Institute, Guangxi Shenguan Collagen Biological Group, Wuzhou, 543000, China
3These authors contributed equally to this work

Received 
29 Aug 2024
Accepted 
21 Feb 2025
Published
26 Feb 2025

Abstract

Proteins are the fundamental building blocks of nature, constructing complex molecular machines and dynamic materials. They form the protein complexes that drive life cycles and the cellular skeletal components and muscle fibers responsible for movements. Due to their extensive molecular diversity, many biomedical and industrial challenges associated with natural proteins remain unsolved. This review presents a comprehensive analysis of the structure and function of fibrous proteins, elastin, and mucins, emphasizing their roles as protein materials. It also explores their diverse applications across food, environmental, and biomedical sectors. Additionally, we focus on strategies for optimizing protein structure, including chemical modifications and molecular design, by comparing current design methods and software to summarize recent technological developments. Finally, we explore the challenges and prospects of applying artificial intelligence to complex protein structure design. This application has the potential to advance the development and application of intricate protein materials, address functional defects or instability in biomedicine, and enhance our understanding of natural protein mechanisms. These interdisciplinary collaborations will pave the way for designing new multifunctional proteins.

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