抗菌肽buforinⅡ结构及其抗菌和抗癌活性研究进展

Research advances in structure and antibacterial and anticancer activities of antimicrobial peptide buforin Ⅱ

抗生素滥用加速了细菌产生抗生素耐药性,抗菌肽作为对抗抗生素耐药细菌的潜在候选药物备受关注。buforinⅡ作为其中一种潜力分子成为目前的研究热点。buforinⅡ的结构类似于阳离子α螺旋抗菌肽,其“螺旋-脯氨酸铰链-双亲性螺旋”的独特结构在抗菌和抗癌等方面起决定性作用。通过截短、替换和拼接等策略对buforinⅡ及其同源肽进行结构改造可获得具有良好抗菌和抗癌作用的衍生肽。同时,对不同物种间buforinⅡ同源肽的对比和分析拓宽了分子改造的思路。本文综述buforinⅡ及其重要衍生肽的结构及其抗菌和抗癌活性等的最新研究进展,为新抗菌肽的挖掘和临床应用提供理论依据。

Antibiotic abuse accelerates antibiotic resistance in bacteria, so antimicrobial peptides have attracted much attention as potential candidates for fighting antibiotic-resistant bacteria. BuforinⅡ, as one of the potential molecules, has become a research hotspot. The structure of buforin Ⅱ is similar to that of the cationic α-helix antimicrobial peptide, and its unique structure of "helix-proline hinge-amphipathic helix" plays a critical role in antibacterial and anti-cancer properties. The structure modification of buforin Ⅱ and its homologous peptides through truncation, substitution and splicing strategies can lead to derivative peptides with good antibacterial and anticancer functions. At the same time, the buforin Ⅱ homologous peptides of different species have been compared and analyzed to advance our understanding of molecular modification. These findings can facilitate the mining and clinical applications of new antimicrobial peptides, and help cope with the increasingly serious problem of antibiotic resistance.