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Characterization of heat-induced aggregates of concanavalin A using fluorescent probes

机译：使用荧光探针表征伴刀豆球蛋白A的热诱导聚集体

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摘要

Proteins are prone to aggregate at high temperature. In order to investigate the heat-induced aggregation, Concanavalin A (Con A) was used as a model protein because disulfide formation doesn't occur throughout the aggregation process. With increasing temperature, fluorescence intensities of 8-anilino-1-naphthalenesulfonate (ANS) and thioflavin T (ThT) showed a maximum at around 45-50℃. After the heating, the fluorescence intensities increased with decreasing temperatures. The enhancement of the fluorescence during cooling implies that the heat-induced aggregates of Con A possess porosity on this surface allowing the binding to fluorescent probes.
机译：蛋白质在高温下易于聚集。为了研究热诱导的聚集，将伴刀豆球蛋白A（Con A）用作模型蛋白，因为在整个聚集过程中不会发生二硫键的形成。随着温度的升高，8-苯胺基-1-萘磺酸盐（ANS）和硫代黄素T（ThT）的荧光强度在45-50℃左右出现最大值。加热后，荧光强度随温度降低而增加。冷却过程中荧光的增强表明，热诱导的Con A聚集体在该表面上具有孔隙，从而可以与荧光探针结合。

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