title: Anti-amyloidogenic behavior and interaction of Diallylsulfide with Human Serum Albumin.
abstract: 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 1.14×103M-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.
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India.
authors.forename: Mohammad Khursheed
authors.initials: MK
authors.lastname: Siddiqi
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India.
authors.forename: Parvez
authors.initials: P
authors.lastname: Alam
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India.
authors.forename: Sumit Kumar
authors.initials: SK
authors.lastname: Chaturvedi
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, Uttar Pradesh, India. Electronic address: rizwanhkhan1@yahoo.com.
authors.forename: Rizwan Hasan
authors.initials: RH
authors.lastname: Khan
mesh_terms: D000498:Allyl Compounds / Q000737:chemistry*; D000682:Amyloid / Q000037:antagonists & inhibitors*; D052160:Benzothiazoles; D001665:Binding Sites; D005456:Fluorescent Dyes / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D062105:Molecular Docking Simulation; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012709:Serum Albumin / Q000037:antagonists & inhibitors / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013440:Sulfides / Q000737:chemistry*; D013816:Thermodynamics; D013844:Thiazoles / Q000737:chemistry
chemical_list: D000498:Allyl Compounds; D000682:Amyloid; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D012709:Serum Albumin; D013440:Sulfides; D013844:Thiazoles; C009462:thioflavin T; C038491:allyl sulfide
keywords: Amyloid; Fluorescence quenching; ThT binding