Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells

Problem statement: We have previously analyzed the interaction of BSA with flavonoidsby using FRET. In this study, the role of BSA on increasing in solubility and on carrying the quercetinderivatives thus enhanced their anticancer efficacy against drug-sensitive and drug-resistant cells wereconducte...

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Main Authors: Choiprasert W., Loetchutinat C., Dechsupa N., Mankhetkorn S.
Format: Article
Language:English
Published: 2014
Online Access:http://www.scopus.com/inward/record.url?eid=2-s2.0-79960151223&partnerID=40&md5=9f8848d186e85527853827adfd6f4fdd
http://cmuir.cmu.ac.th/handle/6653943832/875
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spelling th-cmuir.6653943832-8752014-08-29T09:02:16Z Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells Choiprasert W. Loetchutinat C. Dechsupa N. Mankhetkorn S. Problem statement: We have previously analyzed the interaction of BSA with flavonoidsby using FRET. In this study, the role of BSA on increasing in solubility and on carrying the quercetinderivatives thus enhanced their anticancer efficacy against drug-sensitive and drug-resistant cells wereconducted. Approach: The macroscopic (KD) and microscopic (Kd) binding constant of thecomplexation and the cellular partition of molecules were analyzed using FRET and HPLC method,respectively. Results: The KD values reflex the stability of complexes was in the order of rutin >quercetrin > quercetin. BSA was a suitable carrier of quercetin (KD = 1.68×105M-1) which spontaneously release the molecule into solutions and cells. The substitution of rhamnoside (KD =1.37×105 M-1) and rutinoside (KD = 5.0×104M-1) at C3 yielded an increase in stability of thecomplexes. Rutin was tightly bound to BSA resulting in the changes in mode of action. Conclusion:The macroscopic binding constant was directly influenced on the cellular uptake of molecules and thesuitable range of binding constant was KD≥105M-1 by which the carrier can be useful for increasingthe solubility of drug and also spontaneously release the drug into the solution and cells. © 2010 Science Publications. 2014-08-29T09:02:16Z 2014-08-29T09:02:16Z 2011 Article 15533468 http://www.scopus.com/inward/record.url?eid=2-s2.0-79960151223&partnerID=40&md5=9f8848d186e85527853827adfd6f4fdd http://cmuir.cmu.ac.th/handle/6653943832/875 English
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
language English
description Problem statement: We have previously analyzed the interaction of BSA with flavonoidsby using FRET. In this study, the role of BSA on increasing in solubility and on carrying the quercetinderivatives thus enhanced their anticancer efficacy against drug-sensitive and drug-resistant cells wereconducted. Approach: The macroscopic (KD) and microscopic (Kd) binding constant of thecomplexation and the cellular partition of molecules were analyzed using FRET and HPLC method,respectively. Results: The KD values reflex the stability of complexes was in the order of rutin >quercetrin > quercetin. BSA was a suitable carrier of quercetin (KD = 1.68×105M-1) which spontaneously release the molecule into solutions and cells. The substitution of rhamnoside (KD =1.37×105 M-1) and rutinoside (KD = 5.0×104M-1) at C3 yielded an increase in stability of thecomplexes. Rutin was tightly bound to BSA resulting in the changes in mode of action. Conclusion:The macroscopic binding constant was directly influenced on the cellular uptake of molecules and thesuitable range of binding constant was KD≥105M-1 by which the carrier can be useful for increasingthe solubility of drug and also spontaneously release the drug into the solution and cells. © 2010 Science Publications.
format Article
author Choiprasert W.
Loetchutinat C.
Dechsupa N.
Mankhetkorn S.
spellingShingle Choiprasert W.
Loetchutinat C.
Dechsupa N.
Mankhetkorn S.
Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells
author_facet Choiprasert W.
Loetchutinat C.
Dechsupa N.
Mankhetkorn S.
author_sort Choiprasert W.
title Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells
title_short Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells
title_full Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells
title_fullStr Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells
title_full_unstemmed Relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells
title_sort relation between macroscopic binding constant and the anticancer efficacy of the bovine serum albumin-quercetin complex against drug-sensitive and drug-resistant cells
publishDate 2014
url http://www.scopus.com/inward/record.url?eid=2-s2.0-79960151223&partnerID=40&md5=9f8848d186e85527853827adfd6f4fdd
http://cmuir.cmu.ac.th/handle/6653943832/875
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