@article{ZHAO2023, 
author = {Penghao ZHAO and Jiacui SHANG and Yuhan CHEN and Bofan DUAN and Xiangchen MENG},
title = {A Review of Structural Characteristics and Structure-Function Relationship of Two-Peptide (Class IIb) Bacteriocins},
year = {2023},
journal = {Food Science},
volume = {44},
number = {9},
pages = {170-176},
keywords = {two-peptide bacteriocin, GxxxG motif, structure-activity relationship, helix-helix interaction, aromatic amino acids},
url = {https://www.sciopen.com/article/10.7506/spkx1002-6630-20220227-235},
doi = {10.7506/spkx1002-6630-20220227-235},
abstract = {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.}
}