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Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach

Paper ID Volume ID Publish Year Pages File Format Full-Text
30071 44458 2009 8 PDF Available
Title
Studies on the interaction between imidacloprid and human serum albumin: Spectroscopic approach
Abstract

The interaction between imidacloprid (IMI) and human serum albumin (HSA) was investigated using fluorescence and UV/vis absorption spectroscopy. The experimental results showed that the fluorescence quenching of HSA by IMI was a result of the formation of IMI–HSA complex; static quenching was confirmed to result in the fluorescence quenching. The apparent binding constant KA between IMI and HSA at three differences were obtained to be 1.51 × 104, 1.58 × 104, and 2.19 × 104 L mol−1, respectively. The thermodynamic parameters, ΔH° and ΔS° were estimated to be 28.44 kJ mol−1, 174.76 J mol−1 K−1 according to the van’t Hoff equation. Hydrophobic interactions played a major role in stabilizing the complex. The distance r between donor (HSA) and acceptor (IMI) was obtained according to fluorescence resonance energy transfer. The effect of IMI on the conformation of HSA was analyzed using synchronous fluorescence spectroscopy CD and three-dimensional fluorescence spectra, the environment around Trp and Tyr residues were altered.

Keywords
Imidacloprid; Human serum albumin; Fluorescence spectroscopy; Thermodynamic parameter
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 94, Issue 3, 3 March 2009, Pages 183–190
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
Price after discount Only $4.95
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