期刊
BIOPHYSICAL JOURNAL
卷 81, 期 4, 页码 2203-2214出版社
BIOPHYSICAL SOCIETY
DOI: 10.1016/S0006-3495(01)75868-7
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- NIAID NIH HHS [AI 43934, AI 22839] Funding Source: Medline
- NIGMS NIH HHS [R01 GM066976] Funding Source: Medline
The orientation and dynamics of an 18-residue antimicrobial peptide, ovispirin, has been investigated using solid-state NMR spectroscopy. Ovispirin is a cathelicidin-like model peptide (NH2-KNLRRIIRKIIHIIKKYG-COOH) with potent, broad-spectrum bactericidal activity. N-15 NMR spectra of oriented ovispirin reconstituted into synthetic phospholipids show that the helical peptide is predominantly oriented in the plane of the lipid bilayer, except for a small portion of the helix, possibly at the C-terminus, which deviates from the surface orientation. This suggests differential insertion of the peptide backbone into the lipid bilayer. N-15 spectra of both oriented and unoriented peptides show a reduced N-15 chemical shift anisotropy at room temperature compared with that of rigid proteins, indicating that the peptide undergoes uniaxial rotational diffusion around the bilayer normal with correlation times shorter than 10(-4) s. This motion is frozen below the gel-to-liquid crystalline transition temperature of the lipids. Ovispirin interacts strongly with the lipid bilayer, as manifested by the significantly reduced H-2 quadrupolar splittings of perdeuterated palmitoyloleoylphosphatidylcholine acyl chains upon peptide binding. Therefore, ovispirin is a curved helix residing in the membrane-water interface that executes rapid uniaxial rotation. These structural and dynamic features are important for understanding the antimicrobial function of this peptide.
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