Current Progress in Cross-Linked Peptide Self-Assemblies.

Noriyuki Uchida,Takahiro Muraoka

doi:10.3390/ijms21207577

Noriyuki Uchida, Takahiro Muraoka

Open Access

https://doi.org/10.3390/ijms21207577

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Abstract

Peptide-based fibrous supramolecular assemblies represent an emerging class of biomaterials that can realize various bioactivities and structures. Recently, a variety of peptide fibers with attractive functions have been designed together with the discovery of many peptide-based self-assembly units. Cross-linking of the peptide fibers is a key strategy to improve the functions of these materials. The cross-linking of peptide fibers forming three-dimensional networks in a dispersion can lead to changes in physical and chemical properties. Hydrogelation is a typical change caused by cross-linking, which makes it applicable to biomaterials such as cell scaffold materials. Cross-linking methods, which have been conventionally developed using water-soluble covalent polymers, are also useful in supramolecular peptide fibers. In the case of peptide fibers, unique cross-linking strategies can be designed by taking advantage of the functions of amino acids. This review focuses on the current progress in the design of cross-linked peptide fibers and their applications.

Highlights

There has been a lot of effort to create novel biomaterials applicable to tissue engineering and drug delivery systems
Unique cross-linking methods can be employed by taking advantage of the functionalities of amino acid residues in peptide fibers [79,80,81,82,83,84,85,86,87,88,89,90]
This review focuses on the current progress in cross-linked delivery systems [91,92] have been reported using peptide fiber-based hydrogels with various peptide fibers and thbieoaicrtivaitpieps. lTihcisarteivoienwsf.ocuses on the current progress in cross-linked peptide fibers and their applications

Summary

Introduction

There has been a lot of effort to create novel biomaterials applicable to tissue engineering and drug delivery systems. Self-assembled peptide fibers composed of β-hairpin structures with multiple hydrogen bonds by the introduction of a bend structure derived from repeated proline residues were reported by Schneider (Figure 2c) [58,59,60,61,62,63,64,65,66,67]. J.sMpol.eScci.i2fi020c, 21m, x FeOtRaPlEEiRoRnEVsIEWsuch as arsenic (As) [58]

Effects of Cross-Linking

Non-Covalent Approach

Conclusions