Formation Mechanism and Biomedical Applications of Protease-Manipulated Peptide Assemblies.

Tianyue Jiang,Chendan Liu,Xiao Xu,Bingfang He,Ran Mo

doi:10.3389/fbioe.2021.598050

Abstract

Exploiting enzyme-catalyzed reactions to manipulate molecular assembly has been considered as an attractive bottom-up nanofabrication approach to developing a variety of nano-, micro-, and macroscale structures. Upon enzymatic catalysis, peptides and their derivatives transform to assemblable building blocks that form ordered architecture by non-covalent interactions. The peptide assemblies with unique characteristics have great potential for applications in bionanotechnology and biomedicine. In this mini review, we describe typical mechanisms of the protease-instructed peptide assembly via bond-cleaving or bond-forming reactions, and outline biomedical applications of the peptide assemblies, such as drug depot, sustained release, controlled release, gelation-regulated cytotoxicity, and matrix construction.

Highlights

Bottom-up fabrication is related to a precise control and generation of structures with desired shapes and characteristics starting from smaller dimensions by the self-assembly of atoms or molecules
We describe typical mechanisms of the protease-instructed peptide assembly, and outline biomedical application of the peptide assemblies
A host of proteases with specific catalytic activities in human body have been applied as stimuli to obtain peptide-based building blocks for self-assembly of ordered structures, such as matrix metalloproteinase (MMP), thrombin, and chymotrypsin

Summary

Introduction

Bottom-up fabrication is related to a precise control and generation of structures with desired shapes and characteristics starting from smaller dimensions by the self-assembly of atoms or molecules. A host of proteases with specific catalytic activities in human body have been applied as stimuli to obtain peptide-based building blocks for self-assembly of ordered structures, such as matrix metalloproteinase (MMP), thrombin, and chymotrypsin. The protease-catalyzed hydrolysis of the precursor often leads to removal of hydrophilic moieties and generation of molecular building block that self-assembles by ordered arrangement via non-covalent interactions.

Results

Conclusion