Dynamic turn conformation of a short tryptophan-rich cationic antimicrobial peptide and its interaction with phospholipid membranes.
作者： Matthew Nichols , Miljan Kuljanin , Mostafa Nategholeslam , Tuan Hoang , Shaghayegh Vafaei
DOI: 10.1021/JP4096985
关键词:
摘要: Cationic antimicrobial peptides are promising sources for novel therapeutic agents against multi-drug-resistant bacteria. HHC-36 (KRWWKWWRR) is a simple but effective peptide with similar or superior activity compared several conventional antibiotics. In this biophysical study, unique conformational properties of and some its analogs as well interaction lipid membranes investigated in detail. Circular dichroism (CD) molecular dynamics modeling studies different environments reveal dynamic amphipathic structure composed competing turn conformations free energies lower than that the unfolded state, implying strong influence tryptophan interactions formation turns. CD spectra gel electrophoresis also show evidence self-association aqueous milieu both neutrally negatively charged membrane systems. Isothermal titration calorimetry acrylamide fluorescence quenching experiments emphasize preference vesicles. addition, dye leakage suggest functions through surface-associated mechanism weak lytic bacterial model membranes.
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