Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.

In this work we return to the problem of the determination of ligand-receptor binding stoichiometry and binding constants. In many cases the ligand is a fluorescent dye which has low fluorescence quantum yield in free state but forms highly fluorescent complex with target receptor. That is why many...

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Autores principales:	Irina M Kuznetsova, Anna I Sulatskaya, Olga I Povarova, Konstantin K Turoverov
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e99d26ee52f14569bed3092b9c3310b5
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spelling	oai:doaj.org-article:e99d26ee52f14569bed3092b9c3310b52021-11-18T07:11:53ZReevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.1932-620310.1371/journal.pone.0040845https://doaj.org/article/e99d26ee52f14569bed3092b9c3310b52012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22829890/?tool=EBIhttps://doaj.org/toc/1932-6203In this work we return to the problem of the determination of ligand-receptor binding stoichiometry and binding constants. In many cases the ligand is a fluorescent dye which has low fluorescence quantum yield in free state but forms highly fluorescent complex with target receptor. That is why many researchers use dye fluorescence for determination of its binding parameters with receptor, but they leave out of account that fluorescence intensity is proportional to the part of the light absorbed by the solution rather than to the concentration of bound dye. We showed how ligand-receptor binding parameters can be determined by spectrophotometry of the solutions prepared by equilibrium microdialysis. We determined the binding parameters of ANS - human serum albumin (HSA) and ANS - bovine serum albumin (BSA) interaction, absorption spectra, concentration and molar extinction coefficient, as well as fluorescence quantum yield of the bound dye. It was found that HSA and BSA have two binding modes with significantly different affinity to ANS. Correct determination of the binding parameters of ligand-receptor interaction is important for fundamental investigations and practical aspects of molecule medicine and pharmaceutics. The data obtained for albumins are important in connection with their role as drugs transporters.Irina M KuznetsovaAnna I SulatskayaOlga I PovarovaKonstantin K TuroverovPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e40845 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Irina M Kuznetsova Anna I Sulatskaya Olga I Povarova Konstantin K Turoverov Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.
description	In this work we return to the problem of the determination of ligand-receptor binding stoichiometry and binding constants. In many cases the ligand is a fluorescent dye which has low fluorescence quantum yield in free state but forms highly fluorescent complex with target receptor. That is why many researchers use dye fluorescence for determination of its binding parameters with receptor, but they leave out of account that fluorescence intensity is proportional to the part of the light absorbed by the solution rather than to the concentration of bound dye. We showed how ligand-receptor binding parameters can be determined by spectrophotometry of the solutions prepared by equilibrium microdialysis. We determined the binding parameters of ANS - human serum albumin (HSA) and ANS - bovine serum albumin (BSA) interaction, absorption spectra, concentration and molar extinction coefficient, as well as fluorescence quantum yield of the bound dye. It was found that HSA and BSA have two binding modes with significantly different affinity to ANS. Correct determination of the binding parameters of ligand-receptor interaction is important for fundamental investigations and practical aspects of molecule medicine and pharmaceutics. The data obtained for albumins are important in connection with their role as drugs transporters.
format	article
author	Irina M Kuznetsova Anna I Sulatskaya Olga I Povarova Konstantin K Turoverov
author_facet	Irina M Kuznetsova Anna I Sulatskaya Olga I Povarova Konstantin K Turoverov
author_sort	Irina M Kuznetsova
title	Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.
title_short	Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.
title_full	Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.
title_fullStr	Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.
title_full_unstemmed	Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.
title_sort	reevaluation of ans binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/e99d26ee52f14569bed3092b9c3310b5
work_keys_str_mv	AT irinamkuznetsova reevaluationofansbindingtohumanandbovineserumalbuminskeyroleofequilibriummicrodialysisinligandreceptorbindingcharacterization AT annaisulatskaya reevaluationofansbindingtohumanandbovineserumalbuminskeyroleofequilibriummicrodialysisinligandreceptorbindingcharacterization AT olgaipovarova reevaluationofansbindingtohumanandbovineserumalbuminskeyroleofequilibriummicrodialysisinligandreceptorbindingcharacterization AT konstantinkturoverov reevaluationofansbindingtohumanandbovineserumalbuminskeyroleofequilibriummicrodialysisinligandreceptorbindingcharacterization
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Reevaluation of ANS binding to human and bovine serum albumins: key role of equilibrium microdialysis in ligand - receptor binding characterization.

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