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Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer membranes
- Source :
- Biochemistry. August 2, 2005, Vol. 44 Issue 30, 10208-10217
- Publication Year :
- 2005
-
Abstract
- An 18-residue peptide, KWGAKIKGAKIKIGAKI-NH2 is designed to form amphiphilic beta-sheet structures when bound to lipid bilayers. The peptide possesses high antimicrobial activity when compared to naturally occurring linear antimicrobial peptides, most of which adopt an amphipathic alpha-helical conformation upon binding to the lipids.
Details
- Language :
- English
- ISSN :
- 00062960
- Volume :
- 44
- Issue :
- 30
- Database :
- Gale General OneFile
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.136178886