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A spectral deciphering the perturbation of model transporter protein (HSA) by antibacterial pyrimidine derivative: Pharmacokinetic and biophysical insights

Paper ID Volume ID Publish Year Pages File Format Full-Text
30713 44498 2013 8 PDF Available
Title
A spectral deciphering the perturbation of model transporter protein (HSA) by antibacterial pyrimidine derivative: Pharmacokinetic and biophysical insights
Abstract

Steady state fluorescence and UV–vis absorption spectroscopic techniques have been exploited to explore the binding interaction of a antibacterial pyrimidine derivative 2-amino-6-hydroxy-4-(4-hydroxyphenyl)-pyrimidine-5-carbonitrile (AHHPPC) with the model transporter protein, human serum albumin (HSA) under the physiological conditions. It exhibits antibacterial activity against Escherichia coli and Staphylococcus aureus. Analysis of fluorescence quenching data of HSA at different temperatures using Stern–Volmer methods revealed the formation of AHHPPC–HSA complex with binding affinities of the order 104 M−1. The binding site number (n ≈ 1) and corresponding thermodynamic parameters (ΔG), (ΔH) and (ΔS) were calculated, indicated that binding reaction was endothermic and the hydrophobic interactions plays a major role in stabilizing the complex. The binding distance (r = 3.13 nm) between donor (HSA) and acceptor (AHHPPC) was obtained according to FRET. Changes in the albumin secondary structure imparted by the compound was confirmed using synchronous fluorescence, electronic absorption, circular dichroism (CD) and three-dimensional (3D) fluorescence spectroscopy. All these experimental results clarified that AHHPPC could bind to HSA and be effectively transported and eliminated in body, which could be a useful guideline for further drug design.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Work clarify the pharmokinetics and pharmacodynamics of the antibacterial pyrimidine compound. ► It exhibits antibacterial activity against Escherichia coli and Staphylococcus aureus. ► Study having a great importance in pharmacology and clinical medicine as well as methodology. ► It provides valuable information regarding conformational and microenvironmental changes in protein. ► The experimental results and theoretical data could be useful guideline for further drug design.

Keywords
Fluorescence; Human serum albumin; Fluorescence quenching; Thermodynamic parameters; Pyrimidine derivative
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A spectral deciphering the perturbation of model transporter protein (HSA) by antibacterial pyrimidine derivative: Pharmacokinetic and biophysical insights
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 118, 5 January 2013, Pages 1–8
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