Characteristics and thermodynamics of the interaction of 6-shogaol with human serum albumin as studied by isothermal titration calorimetry

The interaction between 6-shogaol, a pharmacologically active ginger constituent, and human serum albumin (HSA), the main in vivo drug transporter, was investigated using isothermal titration calorimetry (ITC). The value of the binding constant, Ka (5.02 ± 1.37 × 104 M−1) obtained for the 6-shogaol-...

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Published inBrazilian Journal of Pharmaceutical Sciences Vol. 52; no. 3; pp. 443 - 446
Main Authors Feroz, Shevin Rizal, Malek, Sri Nurestri Abdul, Tayyab, Saad
Format Journal Article
LanguageEnglish
Published Sao Paulo Universidade de Sao Paulo Faculdade de Ciencias 01.07.2016
Universidade de São Paulo, Faculdade de Ciências Farmacêuticas
Universidade de São Paulo
Subjects
6-Shogaol
Experiments
Human serum albumin/Isothermal titration calorimetry
Hydrogen bonds
Ligand-protein interaction
Ligands
Metabolism
Metabolites
NMR
Nuclear magnetic resonance
PHARMACOLOGY & PHARMACY
Proteins
Thermodynamics
United States > US
6-Shogaol
Human serum albumin/Isothermal titration calorimetry
Ligand-protein interaction
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Summary:The interaction between 6-shogaol, a pharmacologically active ginger constituent, and human serum albumin (HSA), the main in vivo drug transporter, was investigated using isothermal titration calorimetry (ITC). The value of the binding constant, Ka (5.02 ± 1.37 × 104 M−1) obtained for the 6-shogaol-HSA system suggested intermediate affinity. Analysis of the ITC data revealed feasibility of the binding reaction due to favorable enthalpy and entropy changes. The values of the thermodynamic parameters suggested involvement of van der Waals forces, hydrogen bonds and hydrophobic interactions in the 6-shogaol-HSA complex formation.
ISSN:1984-8250
2175-9790
1984-8250
2175-9790
DOI:10.1590/s1984-82502016000300010