作者
Mohammad Furkan, Md Tauqir Alam, Asim Rizvi, Kashan Khan, Abad Ali, Aabgeena Naeem
发表日期
2017/5/15
期刊
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
卷号
179
页码范围
188-193
出版商
Elsevier
简介
Aggregation of proteins is a physiological process which contributes to the pathophysiology of several maladies including diabetes mellitus, Huntington's and Alzheimer's disease. In this study we have reported that aloe emodin (AE), an anthroquinone, which is one of the active components of the Aloe vera plant, acts as an inhibitor of hemoglobin (Hb) aggregation. Hb was thermally aggregated at 60 °C for four days as evident by increased thioflavin T and ANS fluorescence, shifted congo red absorbance, appearance of β sheet structure, increase in turbidity and presence of oligomeric aggregates. Increasing concentration of AE partially reverses the aggregation of the model heme protein (hemoglobin). The maximum effect of AE was observed at 100 μM followed by saturation at 125 μM. The results were confirmed by UV–visible spectrometry, intrinsic fluorescence, ThT, ANS, congo red assay as well as …
引用总数
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