猪源抗菌肽PMAP-36的序列设计及其结构优化的研究进展

Sequence design and structural optimization of porcine myeloid antimicrobial peptide PMAP-36: a review

摘要:

抗生素的耐药性和动物源性食品中的药物残留问题严重威胁全球公共卫生系统。因此，开发出不易产生耐药性、抗菌活性高的新型抗菌药物迫在眉睫。抗菌肽因其分子量小、抗菌谱广、不易产生耐药性等优点受到科学家们的广泛关注，但天然抗菌肽具有抗菌活性低、溶血活性和细胞毒性等缺陷。随着抗菌肽序列和结构的不断优化，多种具有显著体内外抗菌活性且安全高效的新型抗菌药物被研发出来。猪源抗菌肽PMAP-36是从猪骨髓细胞中分离出来的一种具有典型两亲性α-螺旋结构的高阳离子抗菌肽。本文就国内外关于猪源抗菌肽PMAP-36的序列设计及其结构优化等方面的研究进展进行综述。

Abstract:

Antimicrobial resistance and drug residues in animal-derived foods threaten the global public health. Therefore, it is urgent to develop new antimicrobial drugs with high antimicrobial activity. Antimicrobial peptides (AMPs) have attracted much attention due to their small molecular weight, broad-spectrum antimicrobial activity, and low induced resistance. However, natural antimicrobial peptides have some defects, such as low antimicrobial activity, hemolytic activity and cytotoxicity. With the continuous optimization of antibacterial peptides sequence and structure, a variety of safe and efficient new antibacterial drugs with significant antibacterial activity in vivo and in vitro have been developed. PMAP-36 is a high cationic antimicrobial peptide with typical amphiphilic α-helical structure isolated from porcine bone marrow. In this paper, we review the advance in sequence design and structural optimization of porcine antimicrobial peptide PMAP-36.