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Synthesis, characterization and interaction studies of copper based drug with Human Serum Albumin (HSA): Spectroscopic and molecular docking investigations

Paper ID Volume ID Publish Year Pages File Format Full-Text
30751 44500 2012 8 PDF Available
Title
Synthesis, characterization and interaction studies of copper based drug with Human Serum Albumin (HSA): Spectroscopic and molecular docking investigations
Abstract

A new water soluble copper(II) complex, [Cu(glygly)(ssz)(H2O)]⋅6H2O, 1 derived from dipeptide (glycyl glycine anion) and sulfasalazine was synthesized and characterized by elemental analysis (CHN), molar conductance measurements and spectroscopic methods (IR, UV–vis, ESI-MS). The complex 1 is non-ionic in nature and possess octahedral geometry around Cu(II) metal ion. The interaction of complex 1 with Human Serum Albumin (HSA) was investigated under physiological condition in Tris–HCl buffer solution at pH 7.4 by means of various spectroscopic methods (fluorescence, CD and FTIR) and molecular docking technique. The results of fluorescence titration revealed that the complex 1 strongly quench the intrinsic fluorescence of HSA through a static quenching procedure. Binding constants (Kb) and the number of binding sites (n ≈ 1) were calculated using modified Stern–Volmer equations. The thermodynamic parameters ΔG at different temperatures were calculated subsequently the value of ΔH and ΔS was also calculated which revealed that the hydrophobic and hydrogen bonding interactions play a major role in HSA–complex 1 association. The distance r between donor (HSA) and acceptor (complex 1) was obtained according to fluorescence resonance energy transfer and the alterations of HSA secondary structure induced by complex 1 were confirmed by FT-IR and CD measurements.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The interaction of complex 1 with HSA was investigated by spectroscopic and molecular docking techniques. ► The secondary structure of protein has been changed upon the interaction with complex 1. ► Complex 1 quenched the fluorescence of HSA through static quenching mechanism. ► Site I of the protein is found to be the main binding site for complex 1.

Keywords
Human Serum Albumin (HSA); Fluorescence quenching; Molecular modeling; Fourier transformation infrared spectra (FT-IR); Sulfa drugs
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Synthesis, characterization and interaction studies of copper based drug with Human Serum Albumin (HSA): Spectroscopic and molecular docking investigations
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 114, 3 September 2012, Pages 132–139
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us