Journal
JOURNAL OF THE CHINESE CHEMICAL SOCIETY
Volume 56, Issue 5, Pages 961-966Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/jccs.200900140
Keywords
Antimicrobial peptide; Micelle; CD; Fluorescence; NMR; Structure
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Funding
- NTHU-Pacgen commissioned research project
- National Science Council, ROC [NSC97-2321-B-007-002, NSC97-2311-B-007-008-MY3]
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P-113, AKRHHGYKRKFH-NH2, was derived from human saliva and found to possess clinical activity against fungus infections in HIV patients with oral candidiasis. We have determined the solution structure of P-113 bound to membrane-mimetic SDS micelles by two-dimensional NMR methods. The SDS micelle-bound structure of P-113 adopts an alpha-helical segment and the positively charged residues are clustered together to form a hydrophilic patch. A variety of biophysical and biochemical experiments, including circular dichroism, fluorescence spectroscopy and microcalorimetry, were used to show that P-113 interacted with negatively charged phospholipid vesicles and induced dye release from these vesicles. However, its dye leakage efficiency is much less than the results of previously reported antimicrobial peptides. These results suggest that the antimicrobial activity of P-113, unlike other antimicrobial peptides, may act not only through binding to and destabilization of the microbial membrane but also through a specific protein receptor on the microbial cell surface.
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