Vanillin restrains non-enzymatic glycation and aggregation of albumin by chemical chaperone like function

被引:45
作者
Awasthi, Saurabh [1 ]
Saraswathi, N. T. [1 ]
机构
[1] SASTRA Univ, Sch Chem & Biotechnol, Mol Biophys Lab, Thanjavur 613401, Tamil Nadu, India
关键词
Vanillin; Glycation; Aggregation; HUMAN SERUM-ALBUMIN; END-PRODUCTS; HOLO-TRANSFERRIN; THIOFLAVIN T; BINDING; MECHANISM; QUANTIFICATION; HYPERGLYCEMIA; CONFORMATION; ENDPRODUCTS;
D O I
10.1016/j.ijbiomac.2016.02.041
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Vanillin a major component of vanilla bean extract is commonly used a natural flavoring agent. Glycation is known to induce aggregation and fibrillation of globular proteins such as albumin, hemoglobin. Here we report the inhibitory potential of vanillin toward early and advanced glycation modification and amyloid like aggregation of albumin based on the determination of both early and advanced glycation and conformational changes in albumin using circular dichroism. Inhibition of aggregation and fibrillation of albumin was determined based on amyloid specific dyes i.e., Congo red and Thioflavin T and microscopic imaging. It was evident that vanillin restrains glycation of albumin and exhibits protective effect toward its native conformation. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:1 / 6
页数:6
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