Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches.

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ID: 3061
2019
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Ranked #6 of 22 articles by views in Luminescence : the journal of biological and chemical luminescence

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Abstract
The interaction of four benzothiazole tethered triazole analogues (MS43, MS70, MS71, and MS78) with human serum albumin (HSA) was investigated using various spectroscopic techniques (ultraviolet-visible (UV-vis) light absorption, fluorescence, circular dichroism (CD), molecular docking and density functional theory (DFT) studies). Fluorescence quenching constants (~10 ) revealed a static mode of quenching and binding constants (K ~10 ) indicating the strong affinity of these analogues for HSA. Further alteration in the secondary structure of HSA in the presence of these analogues was also confirmed by far UV-CD spectroscopy. The intensity loss in CD studied at 222 nm indicated an increase in random coil/β-sheet conformations in the protein. Binding energy values (MS71 (-9.3 kcal mol ), MS78 (-8.02 kcal mol ), MS70 (-7.16 kcal mol ) and MS43 (-6.81 kcal mol )) obtained from molecular docking revealed binding of these analogues with HSA. Molecular docking and DFT studies validated the experimental results, as these four analogues bind with HSA at site II through hydrogen bonding and hydrophobic interactions.
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yadav2019insightluminescence Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Yadav, Priyanka;Kumar Yadav, Jitendra;Dixit, Arvind Kumar;Agarwal, Alka;Kumar Awasthi, Satish;
Journal Luminescence : the journal of biological and chemical luminescence
Year 2019
DOI
10.1002/bio.3676
URL
Keywords Keywords not found

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