NMR paper Study of interaction of human serum albumin with curcumin by NMR and docking.

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[NMR paper] Study of interaction of human serum albumin with curcumin by NMR and docking.

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Side-chains:

NOEs:

Structure from NMR restraints:

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Rosetta-NMR (Robetta)

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GeNMR

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Torsion angles from chemical shifts:

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Promega- Proline

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CSI (via RCI server)

TALOS

MICS caps, β-turns

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HADDOCK

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07-18-2014, 01:02 PM

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Study of interaction of human serum albumin with curcumin by NMR and docking.

Study of interaction of human serum albumin with curcumin by NMR and docking.

Study of interaction of human serum albumin with curcumin by NMR and docking.

J Mol Model. 2014 Aug;20(8):2365

Authors: Singh DV, Bharti SK, Agarwal S, Roy R, Misra K

Abstract
Curcumin has been reported to be therapeutically active but has poor bioavailability, half life, and high rate of metabolic detoxifcation. Most of the hydrophobic and acidic drugs get transported through human serum albumin (HSA). Binding of drugs to serum protein increases their half-life. The present study is focused to analyze interaction of curcumin with HSA by NMR and docking studies. In order to investigate the binding affinity of curcumin with HSA, NMR based diffusion techniques and docking study have been carried out. We report that curcumin has shown comparable binding affinity value vis-a-vis standard, the accessible surface area (ASA) of human serum albumin (uncomplexed) and its docked complex with curcumin at both binding sites was calculated and found to be close to that of warfarin and diazepam respectively. Conclusion drawn from our study demonstrates that curcumin interacts with HSA strongly thereby its poor half life is due to high rate of its metabolic detoxification as reported in literature.

PMID: 25031079 [PubMed - in process]

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