Disulfide crosslinking and helical coiling of peptide micelles facilitate the formation of a printable hydrogel. Issue 18 (8th April 2019)

• Record Type: Journal Article
• Authors: Yang, Xin; Wang, Yuefei; Qi, Wei; Xing, Ruizhe; Yang, Xuejiao; Xing, Qiguo; Su, Rongxin; He, Zhimin
• Is Part Of: Journal of materials chemistry. Volume 7:Issue 18(2019)
• Page Start: 2981
• Page End: 2988
• Publication Date: 2019-04-08
• Subjects: Materials -- Periodicals; Chemistry, Analytic -- Periodicals; Biomedical materials -- Research -- Periodicals; 543.0284
• DOI: 10.1039/c8tb03121e
• Languages: English
• ISSNs: 2050-750X

Abstract

Abstract : Tripeptides self-assembled into aligned micelles which transformed into nanohelices via covalent and noncovalent interactions to give a printable hydrogel. Abstract : We report that the helical coiling of micelles induced by disulfide crosslinking in a lyotropic peptide liquid crystal leads to the formation of a printable hydrogel. The (9-fluorenylmethyloxycarbonyl)-protected phenylalanine–phenylalanine–cysteine tripeptide could firstly self-assemble into aligned micelles at high pH values via noncovalent interactions, leading to the formation of a viscous solution. Intriguingly, the cross-linking of the sulfhydryl group between the peptides changed greatly the rheological properties of the peptide solutions, leading to a 6500-fold increase of the storage modulus to 39 kPa. This led to the formation of a self-supporting peptide hydrogel with a series of improved physical properties, including shear-thinning and thixotropy. The formation of the peptide hydrogels with enhanced physical properties can be attributed to the structural transition of the parallelly aligned worm-like micelles into coiled nanohelices induced by the cross-linking of disulfide bonding. The findings deepen our understanding on the relationship between micelle chirality and gel properties, and provide a strategy to fabricate highly functional materials via simultaneous noncovalent and covalent polymerizations.