Design of an α-helical antimicrobial peptide with improved cell-selective and potent anti-biofilm activity.

ABSTRACT: AR-23 is a melittin-related peptide with 23 residues. Like melittin, its high α-helical amphipathic structure results in strong bactericidal activity and cytotoxicity. In this study, a series of AR-23 analogues with low amphipathicity were designed by substitution of Ala1, Ala8 and Ile17 with positively charged residues (Arg or Lys) to study the effect of positively charged residue distribution on the biological viability of the antimicrobial peptide. Substitution of Ile17 on the nonpolar face with positively charged Lys dramatically altered the hydrophobicity, amphipathicity, helicity and the membrane-penetrating activity against human cells as well as the haemolytic activity of the peptide. However, substitution on the polar face only slightly affected the peptide biophysical properties

SUBMITTER: Zhang SK 

PROVIDER: S-EPMC4897634 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature