Characteristics and thermodynamics of the interaction of 6-shogaol with human serum albumin as studied by isothermal titration calorimetry
Braz. j. pharm. sci
;
52(3): 443-446, July-Sept. 2016. tab, graf
Article
in English
| LILACS
| ID: biblio-828257
ABSTRACT
ABSTRACT 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.
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Index:
LILACS (Americas)
Main subject:
Thermodynamics
/
Ginger
Language:
English
Journal:
Braz. j. pharm. sci
Year:
2016
Type:
Article
/
Project document
Affiliation country:
Malaysia
Institution/Affiliation country:
University of Malaya/MY
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