Document Detail


A thermodynamic characterization of the interaction of 8-anilino-1-naphthalenesulfonic acid with native globular proteins: the effect of the ligand dimerization in the analysis of the binding isotherms.
MedLine Citation:
PMID:  20687233     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
8-Anilino-1-naphthalenesulfonic acid (ANS) is a popular fluorescence probe, broadly used for the analysis of proteins, but the nature of its interaction with proteins and the high increase in the fluorescence intensity that takes place upon such process are still unclear. In the last few years, isothermal titration calorimetry has been used to characterize the nature of the interaction of this dye with proteins. The analysis of the binding isotherms of these studies has not considered the dimerization equilibrium of ANS, which is pH dependent, and it can result in serious errors in the data analysis. In the present work we have developed a suitable data analysis by which this process is taken into account. To study the binding of the dye to proteins at different pH values, we have used the Abl-SH3 domain. Our results suggest that at pH 3 and 5, where the dimerization of the ANS is important, electrostatic interactions are significant for the binding of ANS to the Abl-SH3 domain. However, at pH 7, ANS behaves mostly as monomer and the interaction with the protein is mainly hydrophobic. The pH dependent behavior of the ANS binding to proteins can be explained in terms of ionization states of both, the protein and the ANS. Copyright © 2010 John Wiley & Sons, Ltd.
Authors:
Montserrat Andujar-Sánchez; Vicente Jara-Perez; Eva S Cobos; Ana Cámara-Artigas
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of molecular recognition : JMR     Volume:  24     ISSN:  1099-1352     ISO Abbreviation:  J. Mol. Recognit.     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-04-07     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9004580     Medline TA:  J Mol Recognit     Country:  England    
Other Details:
Languages:  eng     Pagination:  548-56     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 John Wiley & Sons, Ltd.
Affiliation:
Departamento de Química-Física, Bioquímica y Química Inorgánica, Universidad de Almería, Carretera Sacramento, 04120 Almería, Spain. mandujar@ual.es.
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