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Parasin I is a 19-amino acid histone H2A-derived peptide isolated from the skin of the catfish, and shows antimicrobial activity.

Parasin I with comparable antimicrobial activities localized to the cell membrane and subsequently permeabilized the outer and cytoplasmic membranes. Parasin I and its active analogs show strong cytoplasmic membrane permeabilizing activity[1]. Codon optimized parasin I fused with human lysozyme is expressed in Pichia pastoris, and has potent antibiotic activity[2].

[1]. Koo YS, et al. Structure-activity relations of parasin I, a histone H2A-derived antimicrobial peptide. Peptides. 2008 Jul;29(7):1102-8. [2]. Zhao H, et al. Characterization of bioactive recombinant antimicrobial peptide parasin I fused with human lysozyme expressed in the yeast Pichia pastoris system. Enzyme Microb Technol. 2015 Sep;77:61-7.

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