| Autor: |
ZHAO Penghao, SHANG Jiacui, CHEN Yuhan, DUAN Bofan, MENG Xiangchen |
| Jazyk: |
English<br />Chinese |
| Rok vydání: |
2023 |
| Předmět: |
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| Zdroj: |
Shipin Kexue, Vol 44, Iss 9, Pp 170-176 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
1002-6630 |
| DOI: |
10.7506/spkx1002-6630-20220227-235 |
| Popis: |
The two-peptide (class IIb) bacteriocins are generally thermostable small-molecule (< 10 kDa) two-component antimicrobial peptides produced by Gram-positive bacteria. This class of peptides mainly rely on peptide-peptide interactions mediated by typical motifs to form active dimeric transmembrane proteins. Numerous studies have shown that two-peptide bacteriocins have reliable safety and desirable bacteriostatic effect, holding great potential in the control of drug-resistant bacteria. Therefore, the structural features and action mechanisms of two-peptide bacteriocins have received considerable research attention. From the perspectives of the structure formation of two-peptide bacteriocins, peptide-peptide interaction, and peptide-membrane interaction, this article summarizes the mechanism of action of this class of antimicrobial peptides. Meanwhile, the structural regularity of two-peptide bacteriocins and the structural features affecting their activities are elaborated by synthesizing current research. This review will provide new ideas for future research on two-peptide bacteriocins. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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