Computational study for binding of oscillarin to human α-thrombin

Emilia L. Wu, Keli Han, John Z.H. Zhang

Research output: Contribution to journalArticle

Abstract

Quantum mechanical calculation and molecular dynamics simulation have been carried out to study binding of Oscillarin (OSC), an antithrombotic marine natural product to human α-thrombin. The binding interaction energies between the inhibitor and individual protein fragments are calculated using a combination of HF and DFT methods. Study shows that the strong binding of OSC to Asp189, Ser214, Trp215, Gly216, and Gly219 is the primary mechanism of drug binding to thrombin. The individual residueligand interaction energies provide detailed quantitative information about specific residue interaction with the ligand that should be extremely useful to our understanding of the molecular nature of proteinligand binding.

Original languageEnglish (US)
Pages (from-to)551-560
Number of pages10
JournalJournal of Theoretical and Computational Chemistry
Volume8
Issue number4
DOIs
StatePublished - Aug 2009

Keywords

  • MFCC
  • Molecular dynamics
  • Oscillarin
  • Thrombin

ASJC Scopus subject areas

  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Computational Theory and Mathematics

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