Role of Arginine and Lysine in the Antimicrobial Mechanism of Histone-derived Antimicrobial Peptides

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2015 Nov 12

PMID 26555191

Citations 69

Authors

Kara J Cutrona

Bethany A Kaufman

Dania M Figueroa

Donald E Elmore

Affiliations

Soon will be listed here.

Abstract

Translocation of cell-penetrating peptides is often promoted by increased content of arginine or other guanidinium groups. However, relatively little research has considered the role of these functional groups on antimicrobial peptide activity. This study compared the activity of three histone-derived antimicrobial peptides-buforin II, DesHDAP1, and parasin-with variants that contain only lysine or arginine cationic residues. These peptides operate via different mechanisms as parasin causes membrane permeabilization while buforin II and DesHDAP1 translocate into bacteria. For all peptides, antibacterial activity increased with increased arginine content. Higher arginine content increased permeabilization for parasin while it improved translocation for buforin II and DesHDAP1. These observations provide insight into the relative importance of arginine and lysine in these antimicrobial peptides.

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