双肽（IIb类）细菌素的结构特点及其与功能的关系

双肽（IIb类）细菌素通常是由革兰氏阳性菌产生的热稳定小分子（＜10 kDa）双组分抗菌肽，该类肽能够依靠特定模式基序介导肽-肽互作，形成具有跨膜能力的活性二聚体蛋白。大量研究表明，双肽细菌素具有可靠的安全性和理想的抑菌效果，在耐药菌控制方面有着巨大的应用潜力。因此，双肽细菌素发挥功能的结构特征与作用机制受到研究者们的广泛关注。本文按照双肽细菌素结构形成、肽-肽互作及肽-膜互作的逻辑梳理该类抗菌肽发挥抑菌作用的机制，同时综合现有研究阐述双肽细菌素的结构规律及影响其活性的结构要点，以期为双肽细菌素的相关研究提供新的思路。

A Review of Structural Characteristics and Structure-Function Relationship of Two-Peptide (Class IIb) Bacteriocins

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.