Journal ArticleDOI
Spectroscopic studies on the interaction between methylene blue and bovine serum albumin
TLDR
In this paper, the interaction between methylene blue (MB) and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorbance spectroscopy.Abstract:
The interaction between methylene blue (MB) and bovine serum albumin (BSA) was investigated by fluorescence and UV–vis absorbance spectroscopy. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by MB is mainly a result of the formation of MB–BSA complex and electrostatic interactions play an important role to stabilize the complex. The Stern–Volmer quenching constant K SV and corresponding thermodynamic parameters Δ H , Δ G , and Δ S were calculated. The distance r between donor (BSA) and acceptor (MB) was obtained according to fluorescence resonance energy transfer (FRET). The effect of MB on the conformation of BSA has been analyzed by means of UV–vis absorbance spectra and synchronous fluorescence spectroscopy.read more
Citations
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Journal ArticleDOI
Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods.
TL;DR: The interaction between malachite green and bovine serum albumin (BSA) under simulative physiological conditions was investigated by the methods of fluorescence spectroscopy, UV-vis absorption and circular dichroism (CD) spectroscope, which confirmed some micro-environmental and conformational changes of BSA molecules.
Journal ArticleDOI
Elucidating the interaction of limonene with bovine serum albumin: a multi-technique approach
Sumit Kumar Chaturvedi,Ejaz Ahmad,Javed Masood Khan,Parvez Alam,Mohd Ishtikhar,Rizwan Hasan Khan +5 more
TL;DR: The present study will be helpful in understanding the binding mechanism of limonene and associated stability and conformational changes.
Journal ArticleDOI
Characterization of the baicalein–bovine serum albumin complex without or with Cu2+or Fe3+ by spectroscopic approaches
TL;DR: Results indicate that the binding of baicalein to BSA causes apparent change in the secondary structure of BSA, but does not affect the polarity around the chromophore molecule.
Journal ArticleDOI
Studies of the interaction between paraquat and bovine hemoglobin.
Yanqing Wang,Hongmei Zhang,Gen-Cheng Zhang,Shuang-Xia Liu,Qiu-Hua Zhou,Zhenghao Fei,Zong-Tang Liu +6 more
TL;DR: Hydrophobic and electrostatic interactions played a major role in stabilizing the complex and fluorescence quenching of BHb by PQ was a result of the formation of PQ-BHb complex.
Journal ArticleDOI
Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method.
TL;DR: It was found that both static quenching and non-radiation energy transfer were the main reasons for the fluorescence quenched, and the interaction of puerarin and BSA was driven mainly by hydrophobic forces.
References
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Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Journal ArticleDOI
Zwischenmolekulare Energiewanderung und Fluoreszenz
TL;DR: In this article, a quantenmechanische behandlung des Ubergangs von Elektronenanregungsenergie zwischen gleichartigen Molekulen in Losung gegeben.
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Atomic structure and chemistry of human serum albumin.
Xiao Min He,Daniel C. Carter +1 more
TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.
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Structure of serum albumin.
Daniel C. Carter,Joseph X. Ho +1 more
TL;DR: This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin and suggests that AFP may have a higher affinity for some unknown ligands important for fetal development.
Journal ArticleDOI
Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion.
TL;DR: The results of the model compound study provide evidence for a mechanism that follows the classical Stern-Volmer law (1919), predominantly involving collisional quenching, and illustrate the importance of local charge and solvent viscosity.
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