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Detecting Protein-Glycolipid Interactions using Glycomicelles and CaR-ESI-MS

机译:使用甘料糖和轿车-SI-MS检测蛋白质 - 糖脂相互作用

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High affinity interaction of CTB_5 and GM1 glycomicelle was revealed by CaR-ESI-MS assay. However, the apparent affinity is significantly lower than that of corresponding GM1_(os) or GM1 nanodiscs. No binding of CTB_5 to GM2 or GM3 glycomicelle was observed. In the absence of GM1, very little ganglioside-bound CTB_6 was detected suggesting that CTB_5-ganglioside binding (specific or non-specific) is enhanced by the presence of the high affinity GM1. Nonspecific binding during ESI process could be responsible for CTB_5 interactions with GD1a, GD1b, GT1b and GD2 glycomicelles in that corresponding nonspecific interactions were observed for Stx1B_5.
机译:CAR-ESI-MS测定揭示了CTB_5和GM1 GLYCOMICELLE的高亲和力相互作用。然而,表观亲和力显着低于相应的GM1_(OS)或GM1纳米DISC。没有观察到CTB_5至GM2或GM3甘草晶的结合。在没有GM1的情况下,检测到非常小的神经节苷脂结合的CTB_6,表明通过高亲和力GM1的存在增强了CTB_5-GALLIORE结合(特异性或非特异性)。 ESI过程中的非特异性结合可能对CTB_5与GD1A,GD1B,GT1B和GD2颗粒的相互作用负责,即在STX1B_5观察到对应的非特异性相互作用。

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