人血清白蛋白
化学
动态光散射
荧光
荧光光谱法
圆二色性
生物物理学
对接(动物)
差示扫描量热法
结晶学
生物化学
材料科学
纳米技术
纳米颗粒
生物
医学
量子力学
热力学
物理
护理部
作者
Mohammad Khursheed Siddiqi,Parvez Alam,Sumit Kumar Chaturvedi,Rizwan Hasan Khan
标识
DOI:10.1016/j.ijbiomac.2016.08.035
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 ÿ 103 M1. UVvisible 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.
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