Biostable hydrogels consisting of hybrid β-sheet fibrils assembled by a pair of enantiomeric peptides

由一对对映异构肽组装而成的杂化β-折叠纤维构成的生物稳定水凝胶

阅读:1

Abstract

The assembly of chiral peptides facilitates the formation of diverse supramolecular structures with unique physicochemical and biological properties. However, the effects of chirality on peptide assembly and resulting hydrogel properties remain underexplored. In this study, we systematically investigated the assembly propensity, morphology, and biostability of mixture of a pair of enantiomeric peptides (L)E(L)C(L)A(L)F(L)F (ECF-5) and (D)E(D)C(D)A(D)F(D)F (ecf-5) at various ratios. Results indicate the development of β-sheet fibrils, ultimately leading to the formation of self-supporting hybrid hydrogels. The hydrogel formed at a ratio of 1:1 exhibits a significantly lower storage modulus (G') than of the ratios of 0:1, 1:3, 3:1 and 1:0 (n(D)/n(L); same below). Kink-separated fragments of approximately 100 nm in length predominate at ratios of 1:3 and 3:1, compared with the smooth fibrils at other ratios, probably attributed to an alternating arrangement of the co-assembled and self-assembled peptide fragments. The introduction of ecf-5 to the hybrid hydrogels improves resistance to proteolytic digestion and maintains commendable biocompatibility in both MIN6 and HUVECs cells. These findings provide valuable insights into the development of hydrogels with tailored properties, positing them potential scaffolds for 3D cell culture and tissue engineering.

特别声明

1、本页面内容包含部分的内容是基于公开信息的合理引用;引用内容仅为补充信息,不代表本站立场。

2、若认为本页面引用内容涉及侵权,请及时与本站联系,我们将第一时间处理。

3、其他媒体/个人如需使用本页面原创内容,需注明“来源:[生知库]”并获得授权;使用引用内容的,需自行联系原作者获得许可。

4、投稿及合作请联系:info@biocloudy.com。