Role of arginine and lysine in the antimicrobial mechanism of histone‐derived antimicrobial peptides
Year: 2015
Type: article
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.
Source: FEBS Letters
Institution: Wellesley College
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: bronze
Awards: G1857588929, MRI:Acquisition of a Circular Dichroism Spectrophotometer for Interdisciplinary Research and Training in Chemistry and Biology at an Undergraduate College, REU Site: Chemistry as the Focus of an Interdisciplinary Summer Research Program at Wellesley College, Characterization and Design of Histone-Derived Antimicrobial Peptides
OpenAlex ID: W2123231250