期刊
CHEMISTRY AND PHYSICS OF LIPIDS
卷 107, 期 1, 页码 83-92出版社
ELSEVIER SCI IRELAND LTD
DOI: 10.1016/S0009-3084(00)00153-5
关键词
HIV envelope glycoprotein; lipid monolayer; film balance; lipid-peptide interaction; electrostatic interaction
The interaction of a peptide identical to the carboxy terminal region of the envelope glycoprotein gp41(828) of HIV with negatively charged phospholipids in a monolayer was studied by a Wilhelmy film balance. No significant interaction of the peptide with a monolayer composed of pure neutral but a strong affinity to negatively charged phospholipids could be observed. In mixed phospholipid monolayers the binding of the gp41(828) is primarily limited by the amount of acidic phospholipids. The physical state of the monolayer is another important parameter for binding. Clustering of negatively charged phospholipids and the surface pressure are crucial. Ca2+ ions strongly interfere with the peptide-lipid interaction up to complete abolishment. The effects observed are dependent on the nature of the acidic lipid. Phosphatidylglycerol was found to be more sensitive than phosphatidylserine. The significance of the results for processes like virus assembly and budding will be discussed. (C) 2000 Elsevier Science Ireland Ltd. Ail rights reserved.
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