The binding of two bio-active flavonoids, quercetin and rutin, with bovine hemoglobin was investigated by multi-spectroscopic and computational studies
2018
Molecular recognition of bio-active flavonoids quercetin and rutin by bovine hemoglobin: an overview of the binding mechanism, thermodynamics and structural aspects through multi-spectroscopic and molecular dynamics simulation studies
Key concepts
Scholarcy highlights
- The binding of two bio-active flavonoids, quercetin and rutin, with bovine hemoglobin was investigated by multi-spectroscopic and computational studies
- The two flavonoids were found to quench the intrinsic fluorescence of BHb through a static quenching mechanism
- The binding constants at 288 K were observed to be × 104 M−1 and × 104 M−1, respectively for quercetin and rutin binding with BHb
- Both rutin and quercetin were observed to increase the polarity around the Trp residues of BHb as indicated by synchronous and 3D spectral studies
- Excellent correlations with the experimental studies were observed from the molecular docking and molecular dynamics simulation studies
- Further investigations established that these flavonoids are efficient in the inhibition of glucose mediated glycation of BHb
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