Structural location determines functional roles of the basic amino acids of KR-12, the smallest antimicrobial peptide from human cathelicidin LL-37.

ABSTRACT: Cationic antimicrobial peptides are recognized templates for developing a new generation of antimicrobials to combat superbugs. Human cathelicidin LL-37 is an essential host defense molecule in human innate immunity. Previously, we identified KR-12 as the smallest antibacterial peptide of LL-37. KR-12 has a narrow activity spectrum since it is active against Gram-negative Escherichia coli but not Gram-positive Staphylococcus aureus. The functional roles of the basic amino acids of KR-12, however, have not yet been elucidated. An alanine scan of cationic amino acids of KR-12 provided evidence for their distinct roles in the activities of the peptides. Bacterial killing and membrane permeation experiments indicate that the R23A and K25A mutants, as well as the lysine-to-arginin

SUBMITTER: Mishra B 

PROVIDER: S-EPMC3844289 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature