| Literature DB >> 17368034 |
Xuan Shao1, Yanfeng Gao, Chuanjun Zhu, Xuehui Liu, Jinlong Yao, Yuxin Cui, Rui Wang.
Abstract
We investigated a series of conformations of endomorphin-2 (EM-2) analogs substituted by phenylglycine (Phg) and homophenylalanine (Hfe) in the position 3 or 4 by two-dimensional (1)H NMR spectroscopy and molecular modeling. Evaluating the aromatic interactions and the dihedral angles in these phenylalanine mimics, we have observed that the conformations in trans isomer have varied from extended to folded as bioactivity decreases. It is suggested that the flexibility of aromatic side chain affects the backbone of EM-2 to adopt folded structures, which may block the ligands in binding to micro-opioid receptor.Entities:
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Year: 2007 PMID： 17368034 DOI： 10.1016/j.bmc.2007.02.050
Source DB: PubMed Journal: Bioorg Med Chem ISSN： 0968-0896 Impact factor: 3.641