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

Durg Vijay Singh, Santosh Kumar Bharti, Shikha Agarwal, Raja Roy, Krishna Misra

Research output: Contribution to journalArticlepeer-review

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 serumprotein 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.

Original languageEnglish (US)
Article number2365
JournalJournal of Molecular Modeling
Volume20
Issue number8
DOIs
StatePublished - Aug 2014
Externally publishedYes

Keywords

  • Albumin
  • Computational simulation
  • Curcumin
  • Diffusion NOE pumping
  • Human serum
  • NMR

ASJC Scopus subject areas

  • Catalysis
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Computational Theory and Mathematics
  • Inorganic Chemistry

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