title: Role of peptide self-assembly in antimicrobial peptides.
abstract: Antimicrobial peptides (AMPs) are considered as potential antibiotic substitutes because of their potent activities. Previous studies mainly focused on the effects of peptide charges and secondary structures, but the self-assembly of AMPs was neglected. As more and more researchers notice the roles of peptide self-assembly in AMPs, it has been considered as another important property. In this review, we will discuss the influences of peptide self-assembly on the activity and mode of action, and some specific features it introduces to the AMPs, such as particular responsiveness, improved cell selectivity and stability and sustained release. In addition, some methods to design self-assembling AMPs are primarily discussed. With further understanding about the self-assembling regularity, design of particular self-assembling AMPs will be very helpful for their applications, especially in the fields of drug delivery and biomedical engineering.
authors.affiliation: Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China.
authors.forename: Xibo
authors.initials: X
authors.lastname: Tian
authors.affiliation: Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China.
authors.forename: Fude
authors.initials: F
authors.lastname: Sun
authors.affiliation: Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China.
authors.forename: Xi-Rui
authors.initials: XR
authors.lastname: Zhou
authors.affiliation: Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China.
authors.forename: Shi-Zhong
authors.initials: SZ
authors.lastname: Luo
authors.affiliation: Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China.
authors.forename: Long
authors.initials: L
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D001698:Biomedical Engineering; D016503:Drug Delivery Systems / Q000379:methods*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D049329:Nanostructures / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary; D013004:Somatostatin / Q000031:analogs & derivatives* / Q000737:chemistry; D055672:Static Electricity
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010456:Peptides, Cyclic; C060347:lanreotide; D013004:Somatostatin
keywords: antimicrobial peptides; cell selectivity; drug delivery; peptide self-assembly; stability