A molecular dynamics study on opioid activities of biphalin molecule

Jin Yuan Hsieh, Tzen-Yuh Chiang, Jun Liang Chen, Yun Wen Chen, Hong Chang Lin, Chi-Chuan Hwang

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4 Citations (Scopus)


Molecular dynamics simulations of the biphalin molecule, (Tyr-D-Ala-Gly-Phe-NH) 2, and the active tetrapeptide hydrazide, Tyr-D-Ala-Gly-Phe-NH-NH 2 were performed to investigate the cause of the increased μ and δ receptor binding affinities of the former over the latter. The simulation results demonstrate that the acylation of the two equal tetrapeptide fragments of biphalin produces the constrained hydrazide bridges {\hbox{C}}-4{\alpha } - {{\hbox{C}}-4}\prime - {{\hbox{N}}-9} - {{\hbox{N}}-{{10}}} and {{\hbox{N}}-9} - {{\hbox{N}}-{{10}}} - {{\hbox{C}}-5}\prime - {\hbox{C}}-5{\alpha } , which in turn increase the opportunity of conformations for binding to μ or δ receptors. Meanwhile, the connection of the two active tetrapeptide fragments of biphalin also results in the constrained side chain torsion angle χ 2 at one of the two residues Phe. This constrained side chain torsion angle not only significantly increases the δ receptor binding affinity but also makes most of the δ receptor binding conformations of biphalin bind to the δ receptor through the fragment containing the mentioned residue Phe.

Original languageEnglish
Pages (from-to)2455-2464
Number of pages10
JournalJournal of Molecular Modeling
Issue number10
Publication statusPublished - 2011 Oct 1

All Science Journal Classification (ASJC) codes

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

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