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

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.