Vergne I, Prats M, Tocanne J F, Laneelle G
Laboratoire de Pharmacologie et Toxicologie Fondamentales du CNRS, Toulouse, France.
FEBS Lett. 1995 Nov 20;375(3):254-8. doi: 10.1016/0014-5793(95)01219-5.
Mycobacterial glycopeptidolipid (GPL) interactions with membranes were analysed with monolayer experiment, using GPLs bearing 3, 1, or 0 carbohydrate residues (GPL3, GPL1, GPL0). Compression isotherms and surface potential determinations suggested that the glycopeptidic moiety of GPL3 permanently dipped in water, while those of GPL1 and GPL0 can lay in the interface. Insertion of GPL molecules into a preformed phospholipid monolayer was observed using GPL3 or GPL1 dispersions, but not from GPL0. It is postulated that the activity of GPL0 is low due to its failure to become inserted into membranes, as is that of GPL3 owing to its insertion only by its acyl chain. GPL1 is likely to disturb membranes by inserting its glycopeptidic moiety into the interface.
利用单层实验,对分枝杆菌糖肽脂(GPL)与膜的相互作用进行了分析,使用了带有3个、1个或0个碳水化合物残基的GPL(GPL3、GPL1、GPL0)。压缩等温线和表面电位测定表明,GPL3的糖肽部分永久浸入水中,而GPL1和GPL0的糖肽部分可以位于界面中。使用GPL3或GPL1分散体观察到GPL分子插入预先形成的磷脂单层中,但未观察到GPL0的插入。据推测,GPL0的活性较低是因为它未能插入膜中,GPL3也是如此,因为它仅通过其酰基链插入。GPL1可能通过将其糖肽部分插入界面来干扰膜。