A General and Convenient Peptide Self-Assembling Mechanism for Developing Supramolecular Versatile Nanomaterials Based on The Biosynthetic Hybrid Amyloid-Resilin Protein

© 2023 Wiley-VCH GmbH.

Bibliographische Detailangaben
Veröffentlicht in:Advanced materials (Deerfield Beach, Fla.). - 1998. - 36(2024), 4 vom: 23. Jan., Seite e2304364
1. Verfasser: Wu, Junjun (VerfasserIn)
Weitere Verfasser: Zhou, Lin, Peng, Hu, Wang, Zhaojun, Wang, Zhaoshi, Keasling, Jay D, Liu, Shike, Zhou, Guanghong, Ding, Shijie, Wang, Qiong, Wang, Xuejian, Chen, Xinxiu, Lang, Yifei, Xia, Mo, Guan, Xin, Dong, Mingsheng, Zhou, Jingwen, Chen, Jian
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2024
Zugriff auf das übergeordnete Werk:Advanced materials (Deerfield Beach, Fla.)
Schlagworte:Journal Article amyloid functional bionanomaterials proteins self-assembly resilin 61790-52-1 Amyloidogenic Proteins Peptides Amyloid mehr... Biocompatible Materials Hydrogels Insect Proteins
Beschreibung
Zusammenfassung:© 2023 Wiley-VCH GmbH.
Self-assembling peptides are valuable building blocks to fabricate supramolecular biomaterials, which have broad applications from biomedicine to biotechnology. However, limited choices to induce different globular proteins into hydrogels hinder these designs. Here, an easy-to-implement and tunable self-assembling strategy, which employs Ure2 amyloidogenic peptide, are described to induce any target proteins to assemble into supramolecular hydrogels alone or in combination with notable compositional control. Furthermore, the collective effect of nanoscale interactions among amyloid nanofibrils and partially disordered elastomeric polypeptides are investigated. This led to many useful macroscopic material properties simultaneously emerging from one pure protein material, i.e. strong adhesion to any substrates under wet conditions, rapidly self--assembling into robust and porous hydrogels, adaptation to remodeling processes, strongly promoting cell adhesion, proliferation and differentiation. Moreover, he demonstrated this supramolecular material's robust performance in vitro and vivo for tissue engineering, cosmetic and hemostasis applications and exhibited superior performance compared to corresponding commercial counterparts. To the best of his knowledge, few pure protein-based materials could meet such seemingly mutually exclusive properties simultaneously. Such versatility renders this novel supramolecular nanomaterial as next-generation functional protein-based materials, and he demonstrated the sequence level modulation of structural order and disorder as an untapped principle to design new proteins
Beschreibung:Date Completed 26.01.2024
Date Revised 26.01.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1521-4095
DOI:10.1002/adma.202304364