Anti-amyloidogenic behavior and interaction of Diallylsulfide with Human Serum Albumin

被引:70
作者
Siddiqi, Mohammad Khursheed [1 ]
Alam, Parvez [1 ]
Chaturvedi, Sumit Kumar [1 ]
Khan, Rizwan Hasan [1 ]
机构
[1] Aligarh Muslim Univ, Interdisciplinary Biotechnol Unit, Aligarh 202002, Uttar Pradesh, India
关键词
Fluorescence quenching; ThT binding; Amyloid; BINDING INTERACTION; SULFIDE; AGGREGATION; PATHWAY; CIPROFLOXACIN; INHIBITION; DISULFIDE; LYSOZYME; CRYSTAL; INSIGHT;
D O I
10.1016/j.ijbiomac.2016.08.035
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this work, binding of garlic component-Diallysulfide (DAS) with major human blood transport protein, Human Serum Albumin (HSA) and its anti- amyloidogenic behavior has been studied by utilizing various spectroscopic and molecular docking strategies. The HSA exhibit significant reduction in fluorescence intensity upon interaction with DAS. DAS quenches the fluorescence of HSA in concentration dependent manner with binding affinity of 1.14 x 10(3) M-1. UV-visible spectroscopy results confirm the formation of DAS-HSA complex and secondary structure of HSA get stabilized upon complexation with DAS as observed by far UV CD spectroscopy and Differential Scanning Calorimetry. The topology of HSA in absence and presence of DAS was monitored through Dynamic Light Scattering (DLS) technique, inferred that protein becomes more compact in presence of DAS. Further, molecular docking study shows that DAS bind to the nearby site II in subdomain III of HSA. Moreover, effect of DAS was studied on HSA fibrillation process. ThT binding, ANS fluorescence assay, CD measurement, DLS and Transmission Electron Microscopy (TEM) results altogether confirm the anti-amyloidogenic property of DAS. This work will provide biophysical insight into the interaction of DAS with HSA and will help in designing more potential therapeutic strategies against protein aggregation by exploiting other related compounds. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:1220 / 1228
页数:9
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