摘要
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.
原文 | English |
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頁(從 - 到) | 2455-2464 |
頁數 | 10 |
期刊 | Journal of Molecular Modeling |
卷 | 17 |
發行號 | 10 |
DOIs | |
出版狀態 | Published - 2011 十月 1 |
All Science Journal Classification (ASJC) codes
- Physical and Theoretical Chemistry
- Computer Science Applications
- Computational Theory and Mathematics
- Catalysis
- Organic Chemistry
- Inorganic Chemistry