Hierarchical Self-Assembly of Short Peptides: Nanostructure Formation, Function Tailoring, and Applications.

Abstract

This article explores the hierarchical self-assembly of short peptides, which refers to the structured spatial arrangements of these molecules over long distances. This phenomenon is commonly found in nature and has important implications for biological structure and function. Short peptides are preferred for self-assembly because they have the ability to spontaneously create various nanostructures. This process, known as bottom-up assembly, allows for the addition of functional groups at the carboxyl or amine ends of the peptides. These functional groups enable specific functions that are extremely valuable in the fields of biotechnology and biomedicine. This text discusses the basic processes involved in the self-assembly of short peptides, such as the characteristics of amino acid side chains, the categorization of short peptides according to their chemical structure, the influence of intermolecular forces, and the dynamic nature of the self-assembly process. In addition, the paper discusses the various uses of short peptides in the disciplines of biomedicine and optoelectronics, including stimulus-responsive hydrogels, tissue engineering, and drug delivery. The article also suggests rational design principles for controlling the hierarchical self-assembly of short peptides, creating new commercial applications, particularly with functional hydrogels, and offers insights into the future of the discipline.