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首页> 外文期刊>New Journal of Chemistry >Crocin inhibits urea-induced amyloid formation by bovine beta-lactoglobulin
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Crocin inhibits urea-induced amyloid formation by bovine beta-lactoglobulin

机译:Crocin抑制尿布β-乳糖蛋白的尿素诱导的淀粉样蛋白形成

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摘要

beta-Lactoglobulin (beta-LG), a major whey protein, is able to form amyloid fibrillar aggregates, when subjected to urea-induced denaturation at pH 7.0. Crocin, being a polar carotenoid, was used to investigate its influence on the urea-induced unfolding of beta-LG and formation of amyloid fibrils. Crocin was found to stabilize beta-LG structure against urea at pH 7.0 and subsequently inhibited the amyloid fibril formation when challenged with 5 M urea for 2-4 weeks at 37 degrees C, as observed by thioflavin T fluorescence, congo red binding and transmission electron microscopy. The inhibition by crocin on beta-LG amyloid formation in a concentration-dependent manner exhibited a clear correlation between the midpoint of urea denaturation and lag time. Crocin was found to form a complex with beta-LG with K-d of 4 x 10(-7) M and it could be considered a potential therapeutic agent in the treatment of protein aggregation phenomena.
机译:β-乳球蛋白(β-LG)是一种主要的乳清蛋白,在pH值为7.0的尿素诱导变性时,能够形成淀粉样纤维聚集体。藏红花素是一种极性类胡萝卜素,用于研究其对尿素诱导的β-LG去折叠和淀粉样纤维形成的影响。通过硫黄素T荧光、刚果红结合和透射电子显微镜观察,发现藏红花素在pH 7.0下对尿素稳定β-LG结构,随后在37℃下用5 M尿素激发2-4周时抑制淀粉样纤维的形成。藏红花苷对β-LG淀粉样蛋白形成的抑制呈浓度依赖性,表明尿素变性中点与滞后时间之间存在明显的相关性。发现藏红花苷与β-LG形成复合物,K-d为4 x 10(-7)M,可被认为是治疗蛋白质聚集现象的潜在治疗剂。

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