کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2186439 | 1096059 | 2009 | 12 صفحه PDF | دانلود رایگان |

Solid-state NMR has been used to examine the binding of N′-4-[(4-fluorophenyl)benzyl)]chloroeremomycin, a fluorinated analogue of oritavancin, to isolated protoplast membranes and whole-cell sucrose-stabilized protoplasts of Staphylococcus aureus, grown in media containing [1-13C]glycine and l-[ɛ-15N]lysine. Rotational-echo double-resonance NMR was used to characterize the binding by estimating internuclear distances from 19F of oritavancin to 13C and 15N labels of the membrane-associated peptidoglycan and to the 31P of the phospholipid bilayer of the membrane. In isolated protoplast membranes, both with and without 1 M sucrose added to the buffer, the nascent peptidoglycan was extended away from the membrane surface and the oritavancin hydrophobic side chain was buried deep in the exposed lipid bilayer. However, there was no N′-4-[(4-fluorophenyl)benzyl)]chloroeremomycin binding to intact sucrose-stabilized protoplasts, even though the drug bound normally to the cell walls of whole cells of S. aureus in the presence of 1 M sucrose. As shown by the proximity of peptidoglycan-bridge 13C labels to phosphate 31P, the nascent peptidoglycan of the intact protoplasts was confined to the membrane surface.
Journal: Journal of Molecular Biology - Volume 391, Issue 2, 14 August 2009, Pages 414–425