Molecular Modification and Application of Porcine Antimicrobial Peptides
Antimicrobial peptides(AMPs)are small peptides that are commonly found in plants,animals and microorganisms.Most of them exhibit broad-spectrum antibacterial prowess and are considered to be a promis-ing candidate for antibiotics.The porcine AMPs are the first batch isolated from mammals.To data,over 30 porcine AMPs with elucidated sequences have been identified,with the predominant families being Cathelici-dins and defensins.The bactericidal mechanism of these porcine AMPs diverges significantly from conventional antibiotics by interacting directly with the bacterial cell membrane,compromising its impermeability,inducing cellular leakage and culminating in cell death.The non-specific membrane rupture mechanism is not prone to produce drug resistance.However,natural porcine AMPs still have limitations such as poor stability,high cyto-toxicity and prohibitive cost for large-scale production.Researchers have developed methods such as residue substitution,sequence truncation,motif hybridization,structure optimization and/or fatty acid modification to obtain short-sequence AMPs with both efficiency and biocompatibility.This review attempts to categorize por-cine AMPs based on their original classification,while providing a comprehensive overview of their secondary structure,action mechanism,molecular modifications,and prospective applications.[Chinese Journal of Ani-mal Nutrition,2024,36(6):3413-3424]
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