Investigation of the Interaction between Adenosine and Human Serum Albumin by Fluorescent Spectroscopy and Molecular Modeling

Article Details

Citation

Cui F, Wang J, Li F, Fan J, Qu G, Yao X, Lei B

Investigation of the Interaction between Adenosine and Human Serum Albumin by Fluorescent Spectroscopy and Molecular Modeling

Chinese Journal of Chemistry. 2008 Apr 16;26(4):661-665.

PubMed ID
Not Available
Abstract

The binding interaction of adenosine with human serum albumin (HSA) was investigated under simulative physiological conditions by fluorescence spectroscopy in combination with a molecular modeling method. A strong fluorescence quenching reaction of adenosine to HSA was observed and the quenching mechanism was suggested as static quenching according to the Stern‐Volmer equation. The binding constants (K) at different temperatures as well as thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated according to relevant fluorescent data and Vant′Hoff equation. The hydrophobic interaction was a predominant intermolecular force in order to stabilize the complex, which was in agreement with the results of molecular modeling study.

DrugBank Data that Cites this Article

Drugs
Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
AdenosineSerum albuminProteinHumans
Unknown
Binder
Details