Trommeshauser D, Krol S, Bergelson L D, Galla H J
Institute of Biochemistry, Westfälische Wilhelms-Universität Münster, Wilhelm-Kiemm-Strasse 2, 48149 Münster, Germany.
Chem Phys Lipids. 2000 Sep;107(1):83-92. doi: 10.1016/s0009-3084(00)00153-5.
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. Ca(2+) 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.
利用威尔海姆膜天平研究了与HIV包膜糖蛋白gp41（828）羧基末端区域相同的肽与单层中带负电荷磷脂的相互作用。未观察到该肽与由纯中性磷脂组成的单层有明显相互作用，但可观察到其对带负电荷磷脂有很强的亲和力。在混合磷脂单层中，gp41（828）的结合主要受酸性磷脂量的限制。单层的物理状态是结合的另一个重要参数。带负电荷磷脂的聚集和表面压力至关重要。钙离子强烈干扰肽-脂质相互作用，直至完全消除。观察到的效应取决于酸性脂质的性质。发现磷脂酰甘油比磷脂酰丝氨酸更敏感。将讨论这些结果对病毒组装和出芽等过程的意义。
