Document Detail


Influence of stearic acids on resveratrol-HSA interaction.
MedLine Citation:
PMID:  22987139     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The interaction between the natural polyphenol resveratrol and human serum albumin (HSA), the most abundant transport protein in plasma, has been studied in the absence and in the presence of up to six molecules of stearic acids (SA) pre-complexed with the protein. The study has been carried out by using the intrinsic fluorescence of both HSA and resveratrol. Protein and polyphenol fluorescence data indicate that resveratrol binds to HSA with an association constant k(a) = (1.10 ± 0.14) × 10(5) M(-1) and (1.09 ± 0.02) × 10(5) M(-1), respectively, whereas Job plot evidences the formation of an equimolar protein/drug complex. Low SA content associated with HSA does not affect significantly the structural conformation of the protein and its interaction with resveratrol, whereas high SA content induces conformational changes in the protein, and reduces resveratrol binding affinity. The photostability of resveratrol in the different samples changes in the order: buffer < (high [SA]/HSA) < HSA < (low [SA]/HSA). The results on (SA/HSA)-resveratrol samples highlight the ability of the protein to bind hydrophobic and amphiphilic ligands and to protect from degradation an important antioxidant molecule under biologically relevant conditions.
Authors:
Manuela Pantusa; Luigi Sportelli; Rosa Bartucci
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-09-18
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  41     ISSN:  1432-1017     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-10-19     Completed Date:  2013-03-19     Revised Date:  2013-06-03    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  969-77     Citation Subset:  IM    
Affiliation:
Department of Physics and CNISM Unit, University of Calabria, 87036 Rende, Italy. manuela.pantusa@fis.unical.it
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Humans
Molecular Sequence Data
Protein Binding
Protein Interaction Domains and Motifs
Serum Albumin / chemistry*,  metabolism
Stearic Acids / chemistry*,  pharmacology
Stilbenes / chemistry*,  pharmacology
Chemical
Reg. No./Substance:
0/Serum Albumin; 0/Stearic Acids; 0/Stilbenes; Q369O8926L/resveratrol

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