Amphiphilic peptide molecules have amphiphilic properties similar to natural phospholipid molecules, rich molecular structures, unique and novel assembly structures and special biological functions, and are a hot field of research on peptide self-assembly.

As natural excellent assembly molecules, peptides have special biological activities and good biocompatibility, and can endow materials with unique biological functions. Ease of synthesis and chemical modification are also outstanding advantages of peptide molecules.(from custom peptide synthesis Omizzur) Through the arrangement and combination of 20 natural amino acids and the introduction of exogenous functional groups, hundreds of millions of peptide assembly molecules can be provided to form a vast sea of structures and functions. the peptide assembly. It is also an important way to realize the "bottom-up" preparation of new biofunctional materials with nano/submicron structures. Compared with other self-assembly systems, peptide self-assembly has broad application prospects in biomedical fields such as advanced functional material preparation, gene therapy, biomineralization, biosensing, and tissue engineering, and has been studied.

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In the research of peptide self-assembly, the molecular structure and design of peptides as building blocks are very important, which are important factors to determine the self-assembly behavior of peptides and the morphology and function of the assembly. The molecular structure of amphiphilic polypeptides has hydrophobic segments and hydrophilic end groups similar to surfactants. It can self-assemble to form regular and ordered nano/micro structures. During the assembly process, the hydrophobic segments aggregate with each other due to hydrophobicity to form the hydrophobic core of the assembly, and the generated hydrophobic force is the main driving force for the self-assembly of amphiphilic molecules and the maintenance of the structural stability of the assembly; The hydrogen bonds between the peptide chains make the hydrophilic polypeptide segments close to each other closely packed on the surface of the assembly with a specific secondary structure, and contact with water to further drive the completion of the assembly.

There are many kinds of amphiphilic polypeptide molecules. According to the composition of hydrophobic segments, they can be divided into surface active peptides (surfactant-like peptides) whose hydrophobic segments are all composed of amino acid residues and amphiphilic peptides whose hydrophobic chains are long alkyl carbon chains. (Peptide amphiphiles, PAs), and the latter can be divided into traditional amphiphilic peptides and structurally special amphiphilic peptides according to different molecular structures, such as Bola-type amphiphilic peptides and Gemini-type amphiphilic peptides.