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Structural Characterization of Glycosphingolipids and Toxin Receptor Gangliosides by IRMPD with TLC/VC-MALDI-FTMS.

机译:用TLC / VC-MALDI-FTMS的IRMPD结构表征糖磷脂和毒素受体神经糖苷的结构表征。

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Glycosphingolipids and gangliosides participate in diverse biological processes, and their biological roles are dependent on the structures of both the oligosaccharide and the ceramide portions. Here, vibrationally cooled (VC)MALDI-FTMS was used for the detection of labile species followed by their efficient fragmentation by SORI-CAD and IRMPD. GM1 and GD1a gangliosides serve as trafficking receptors for cholera toxin and the related LTIIb toxin, respectively.[1] We assume that GD1a ganglioside of human intestinal cells is not associated with lipid rafts due to its ceramide structural variation, which prevents endocytosis of the LTIIb-GD1a complex.[2] The toxin receptors' ganglioside structures were evaluated as a moderator of this function, including ceramide chain length, level of saturation and hydroxylation, as well as glycan composition. To analyze these molecules, our previously developed method of direct coupling of TLC plates with VC-MALDI-FTMS was used.[3] This allows direct TLC-MALDI-FTMS without adversely affecting the FT high resolution and mass accuracy by the surface irregularity of the TLC plate. Collisional cooling is necessary for stabilization and detection of intact gangliosides.[3-5]
机译:糖磷脂和神经节苷脂参与不同的生物过程,它们的生物学作用取决于寡糖和神经酰胺部分的结构。这里,振动冷却的(VC)MALDI-FTMS用于检测不稳定物种,然后通过Sori-CAD和IRMPD的有效碎片。 GM1和GD1A神经节花苷分别用作霍乱毒素的贩运受体和相关劳替毒素。[1]我们假设由于其神经酰胺结构变异,人肠细胞的GD1A神经植物与脂质筏无关,这可以防止LTIIB-GD1A复合物的内吞作用。[2]毒素受体的神经节苷脂结构被评价为该功能的主体,包括神经酰胺链长度,饱和水平和羟基,以及聚糖组合物。为了分析这些分子,使用先前开发了具有VC-MALDI-FTMS的TLC平板的直接偶联方法。[3]这允许直接TLC-MALDI-FTMS通过TLC板的表面不规则性不利地影响FT高分辨率和质量精度。抗碰撞冷却是稳定和检测完整神经节苷脂的必要条件。[3-5]

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