Correlations between membrane immersion depth, orientation, and salt-resistance of tryptophan-rich antimicrobial peptides
Journal
Biochimica et Biophysica Acta - Biomembranes
Journal Volume
1828
Journal Issue
11
Pages
2720-2728
Date Issued
2013
Author(s)
Yu, Hui-Yuan; Tu, Chih-Hsiang; Chen, Heng-Li; Chu, Hung-Lun; Chih, Ya-Han; Cheng, Hsi-Tsung; Sue, Shih-Che; Cheng, Cheng, Jya-Wei
Abstract
The efficacies of many antimicrobial peptides are greatly reduced in the presence of high salt concentrations therefore limiting their development as pharmaceutical compounds. PEM-2-W5K/A9W, a short Trp-rich antimicrobial peptide developed based on the structural studies of PEM-2, has been shown to be highly active against various bacterial strains with less hemolytic activity. Here, correlations between membrane immersion depth, orientation, and salt-resistance of PEM-2 and PEM-2-W5K/A9W have been investigated via solution structure and paramagnetic resonance enhancement studies. The antimicrobial activities of PEM-2-W5K/A9W and PEM-2 against various bacterial and fungal strains including multidrug-resistant and clinical isolates under high salt conditions were tested. The activities of the salt-sensitive peptide PEM-2 were reduced and diminished at high salt concentrations, whereas the activities of PEM-2-W5K/A9W were less affected. The results indicated that the strong salt-resistance of PEM-2-W5K/A9W may arise from the peptide positioning itself deeply into microbial cell membranes and thus able to disrupt the membranes more efficiently.
SDGs
Type
journal article