Novelin situand rapid self-gelation recombinant collagen-like protein hydrogel for wound regeneration: mediated by metal coordination crosslinking and reinforced by electro-oxidized tea polyphenols.
{"title":"Novel<i>in situ</i>and rapid self-gelation recombinant collagen-like protein hydrogel for wound regeneration: mediated by metal coordination crosslinking and reinforced by electro-oxidized tea polyphenols.","authors":"Yue Sun, Cungang Gao, Pengxin Jia, Liang Song, Jia Kang, Min Han, Wenfa Yu, Rui Nian","doi":"10.1088/1758-5090/ad9408","DOIUrl":null,"url":null,"abstract":"<p><p>Recombinant collagen holds immense potential in the development of medical functional materials, yet its widespread application remains hindered by the absence of a suitable self-assembly strategy. In this article, we report the discovery that the bacterial-derived collagen-like (CL) protein Scl2 can rapidly self-gelation (∼1 min at pH ∼7) due to properties enabled by metal coordination crosslinking. This was achieved by fusing metal ion chelating peptides to both termini of the protein. Our research further reveals the critical role of electrostatic interaction between globular domains (V domains) of recombinant collagen in the self-assembly process. We show that modifying the negative charge load of the N-terminal<i>α</i>-helix of the V domain enables control over the self-assembly time (from 1 min to 30 min) and strength (from 8 kPa to 26 kPa) of the Scl2 hydrogel. By adjusting the molecular weight of the core CL domain, we have remarkably further enhanced the strength of the Scl2 hydrogel to 78 kPa. Moreover, we innovatively employed electro-oxidized tea polyphenols to enhance the stability of the Scl2 hydrogel, resulting in the formation of a reliable self-assembled metal coordination hydrogel at physiological temperature. This approach not only eliminates the need for toxic chemical crosslinking agents but also confers the material with multiple functionalities, such as adhesion, antibacterial, and antioxidant properties. The novel recombinant Scl2 hydrogel exhibited exceptional<i>in situ</i>self-gelation and injectable properties. This innovative hydrogel not only demonstrates remarkable biological activity but also exhibits remarkable tissue repair-promoting capabilities in full-thickness skin injury models (shorten healing cycle by more than 30%). The convenient and versatile nature of this recombinant collagen hydrogel makes it promising for clinical applications in injury treatment, demonstrating broad applications in the future.</p>","PeriodicalId":8964,"journal":{"name":"Biofabrication","volume":" ","pages":""},"PeriodicalIF":8.2000,"publicationDate":"2024-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biofabrication","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1088/1758-5090/ad9408","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"ENGINEERING, BIOMEDICAL","Score":null,"Total":0}
引用次数: 0
Abstract
Recombinant collagen holds immense potential in the development of medical functional materials, yet its widespread application remains hindered by the absence of a suitable self-assembly strategy. In this article, we report the discovery that the bacterial-derived collagen-like (CL) protein Scl2 can rapidly self-gelation (∼1 min at pH ∼7) due to properties enabled by metal coordination crosslinking. This was achieved by fusing metal ion chelating peptides to both termini of the protein. Our research further reveals the critical role of electrostatic interaction between globular domains (V domains) of recombinant collagen in the self-assembly process. We show that modifying the negative charge load of the N-terminalα-helix of the V domain enables control over the self-assembly time (from 1 min to 30 min) and strength (from 8 kPa to 26 kPa) of the Scl2 hydrogel. By adjusting the molecular weight of the core CL domain, we have remarkably further enhanced the strength of the Scl2 hydrogel to 78 kPa. Moreover, we innovatively employed electro-oxidized tea polyphenols to enhance the stability of the Scl2 hydrogel, resulting in the formation of a reliable self-assembled metal coordination hydrogel at physiological temperature. This approach not only eliminates the need for toxic chemical crosslinking agents but also confers the material with multiple functionalities, such as adhesion, antibacterial, and antioxidant properties. The novel recombinant Scl2 hydrogel exhibited exceptionalin situself-gelation and injectable properties. This innovative hydrogel not only demonstrates remarkable biological activity but also exhibits remarkable tissue repair-promoting capabilities in full-thickness skin injury models (shorten healing cycle by more than 30%). The convenient and versatile nature of this recombinant collagen hydrogel makes it promising for clinical applications in injury treatment, demonstrating broad applications in the future.
期刊介绍:
Biofabrication is dedicated to advancing cutting-edge research on the utilization of cells, proteins, biological materials, and biomaterials as fundamental components for the construction of biological systems and/or therapeutic products. Additionally, it proudly serves as the official journal of the International Society for Biofabrication (ISBF).