Molecular self-assembly is ubiquitous in nature and participates in various biological activities to ensure the orderly progress of physiological functions and biochemical reactions of organisms. Peptide self-assembly is an important part of molecular self-assembly, and its excellent biocompatibility provides a new idea for the design of biomedical materials with important application value. In this review, we summarize the main driving forces in the self-assembly process of peptides, briefly introduce the main structures formed by self-assembly of peptides, and discuss in detail the effects of environmental changes (such as pH, temperature, ionic strength, special ions, REDOX state, and light) on the structure and properties of environmentally responsive peptides. At the same time, the application direction and prospect of peptide self-assembly biomaterials are clarified, and it is hoped to provide a reference for subsequent research in this field.
Molecular self-assembly is a spontaneous phenomenon that is ubiquitous in nature. It is closely related to molecular self-assembly from the macroscopic natural landscape to the microscopic formation of DNA double helix structure in cells. There are many kinds of molecules with the ability of self-assembly in nature, including sugars, proteins, phospholipids and nucleic acids. They play a variety of functions in organisms through the aggregation structure formed by self-assembly, which is similar to molecular machines or cellular machines. Self-assembly can not only generate a variety of functional micro-nanostructures, but also form macroscopic supramolecular aggregates visible to the naked eye, such as hydrogels. Peptide self-assembly is an important aspect of molecular self-assembly, and its excellent biocompatibility provides a new idea for the development of biomedical materials with important application value, which has attracted a large number of researchers’ attention in the past decade. These peptides spontaneously assemble and arrange through non-polar amino acids as hydrophobic moieties and polar amino acids as hydrophilic moieties to form highly ordered nanostructures, such as nanospheres, nanotubes, and nanoribbons. These self-assembled structures can also be further integrated to form functional biomaterials with specific structures.
Traditional gel materials are usually prepared by covalent crosslinking and polymerization of small organic molecules. The disadvantages of this method include complex synthesis process, difficulty in material modification, no response to external stimuli, certain cytotoxicity, and difficulty in degradation. These disadvantages severely limit its application. However, the self-assembly of peptides is easier to prepare and modify, and has good biocompatibility and superior degradation properties, which shows great application potential in many fields such as tissue engineering, drug sustained-release materials and antibacterial materials.
Post time: Apr-29-2025