Back to Search
Start Over
Characterization of Diadzein-Hemoglobin Binding using Optical Spectroscopy and Molecular Dynamics Simulations
- Publication Year :
- 2012
-
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 the hydrophobic interactions between ligand and protein, as was observed from spectroscopy. DZN binds between the subunits of HbA, ∼15 A away from the closest heme group of chain α1, emphasizing the fact that the drug does not interfere with oxygen binding site of HbA.
- Subjects :
- Hemoglobin binding
endocrine system diseases
Stereochemistry
Spectrum Analysis
Hemoglobin A
General Medicine
Plasma protein binding
Molecular Dynamics Simulation
Biochemistry
Isoflavones
Article
Hydrophobic effect
chemistry.chemical_compound
Molecular dynamics
chemistry
Structural Biology
Docking (molecular)
Drug delivery
Humans
Thermodynamics
Molecular Biology
Heme
Oxygen binding
Protein Binding
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....f8bff465280e1aa8eae6a3705fdcbb78