Characterization of diadzein-hemoglobin binding using optical spectroscopy and molecular dynamics simulations.

ABSTRACT: The present study establishes the effectiveness of natural drug delivery mechanisms and investigates the interactions between drug and its natural carrier. The binding between the isoflavone diadzein (DZN) and the natural carrier hemoglobin (HbA) was studied using optical spectroscopy and molecular dynamics simulations. The inherent fluorescence emission characteristics of DZN along with that of tryptophan (Trp) residues of the protein HbA were exploited to elucidate the binding location and other relevant parameters of the drug inside its delivery vehicle HbA. Stern-Volmer studies at different temperatures indicate that static along with collisional quenching mechanisms are responsible for the quenching of protein fluorescence by the drug. Molecular dynamics and docking studies supported

SUBMITTER: Sengupta B 

PROVIDER: S-EPMC3409843 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature