Journal ArticleDOI
Comparative spectroscopic studies on drug binding characteristics and protein surface hydrophobicity of native and modified forms of bovine serum albumin: possible relevance to change in protein structure/function upon non-enzymatic glycation.
Reza Khodarahmi,Seyyed Arash Karimi,Mohammad Reza Ashrafi Kooshk,Mohammad Reza Ashrafi Kooshk,Seyyed Abolghasem Ghadami,Seyyed Abolghasem Ghadami,Sirous Ghobadi,Mojtaba Amani +7 more
TLDR
Analysis of the quenching and thermodynamic parameters indicated that intermolecular interactions between drug and albumin may change upon protein modification, and some conformational changes of interacting side chains in subdomain IIA binding site were suggested.About:
This article is published in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy.The article was published on 2012-04-01. It has received 70 citations till now. The article focuses on the topics: Bovine serum albumin & Serum albumin.read more
Citations
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Journal ArticleDOI
Mechanistic and conformational studies on the interaction of food dye amaranth with human serum albumin by multispectroscopic methods.
Guowen Zhang,Yadi Ma +1 more
TL;DR: Analysis of fluorescence spectra indicated that amaranth had a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure, and results of CD and FT-IR spectra showed that binding ofAmaranth to HSA induced conformational changes ofHSA.
Journal ArticleDOI
Spectroscopic study of interaction between osthole and human serum albumin: Identification of possible binding site of the compound
Nooshin Bijari,Yalda Shokoohinia,Mohammad Reza Ashrafi-Kooshk,Samira Ranjbar,Shahram Parvaneh,Maryam Moieni-Arya,Reza Khodarahmi +6 more
TL;DR: The changes in the secondary structure of HSA after its complexation with ligand were studied with CD spectroscopy, which indicate that osthole induced only a slight decrease in the helix structural content of the protein.
Journal ArticleDOI
Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein
Samira Ranjbar,Yalda Shokoohinia,Sirous Ghobadi,Nooshin Bijari,Saeed Gholamzadeh,Nastaran Moradi,Mohammad Reza Ashrafi-Kooshk,Abbas Aghaei,Reza Khodarahmi +8 more
TL;DR: Fluorescence data indicated that isoimperatorin quenches the intrinsic fluorescence of the HSA via a static mechanism and hydrophobic interaction play the major role in the drug binding.
Journal ArticleDOI
Analysis of drug interactions with modified proteins by high-performance affinity chromatography: Binding of glibenclamide to normal and glycated human serum albumin
TL;DR: HPAC can be used as tool for examining the interactions of relatively non-polar drugs like glibenclamide with modified proteins and should lead to a more complete understanding of how glycation can alter the binding of drugs in blood.
Journal ArticleDOI
Quantitation of species differences in albumin-ligand interactions for bovine, human and rat serum albumins using fluorescence spectroscopy: A test case with some Sudlow's site I ligands
TL;DR: It is emphasized that in molecular aspects BSA behaves considerably differently from HSA or from albumins of other species therefore, it is strongly recommended to apply at least some confirmatory measurements when data obtained from other species are attempted to be extrapolated to HSA.
References
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Principles of fluorescence spectroscopy
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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
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Alexander D. MacKerell,D. Bashford,M. Bellott,Roland L. Dunbrack,Jeffrey D. Evanseck,Martin J. Field,Stefan Fischer,Jiali Gao,H. Guo,S. Ha,Diane Joseph-McCarthy,L. Kuchnir,K. Kuczera,F. T. K. Lau,C. Mattos,Stephen W. Michnick,Thien H. Ngo,D. T. Nguyen,B. Prodhom,W. E. Reiher,Benoît Roux,M. Schlenkrich,Jeremy C. Smith,Roland H. Stote,John E. Straub,Masakatsu Watanabe,J. Wiórkiewicz-Kuczera,D. Yin,Martin Karplus +28 more
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SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling.
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TL;DR: An environment for comparative protein modeling is developed that consists of SWISS‐MODEL, a server for automated comparativeprotein modeling and of the SWiss‐PdbViewer, a sequence to structure workbench that provides a large selection of structure analysis and display tools.
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SWISS-MODEL: an automated protein homology-modeling server
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