Design, structure of amphiphilic peptide and its application from single molecule to nanoparticle
Peptides have been widely studied for their good biocompatibility and diverse structural characteristics. Amphiphilic peptides, which have the special structure of hydrophilic one end and hydrophobic the other and self-assembly property, have a wide range of biological functions. Thus amphiphilic pe...
Gespeichert in:
Veröffentlicht in: | Results in engineering 2022-12, Vol.16, p.100747, Article 100747 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | Peptides have been widely studied for their good biocompatibility and diverse structural characteristics. Amphiphilic peptides, which have the special structure of hydrophilic one end and hydrophobic the other and self-assembly property, have a wide range of biological functions. Thus amphiphilic peptides become the focus of this paper. Based on the literature research and our previous study on self-designed amphiphilic peptides, this paper describes the design and structure of three kinds of amphiphilic peptides, and reviews their application in antibacterial, antitumor, tissue regeneration and drug carrier from single molecules to nanoparticles. The relationship between their structures, responsiveness, self-assembly and applications have been well represented. Amphiphilic peptides show significant advantages in smart materials that present a bright development prospect in biomedicine. This review will provide a theoretical basis for the design of functional peptides.
•Introduce three kinds of amphiphilic peptides: surfactant peptides, lipopeptides and polypeptide-polymer conjugates.•Review these amphiphilic peptides' secondary structures, responsiveness and self-assembly, and clarify their relationship.•Summarize these amphiphilic peptides' applications in antimicrobial peptides, tissue regeneration and drug carrier.•Provide strategies for the design of functional peptides. |
---|---|
ISSN: | 2590-1230 2590-1230 |
DOI: | 10.1016/j.rineng.2022.100747 |