Conformational analysis of endomorphin-2 analogs with phenylalanine mimics by NMR and molecular modeling

The conformations of EM-2 analogs varied from extended to folded structure as bioactivity decreases. 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 1H NMR spectroscopy...

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Veröffentlicht in:	Bioorganic & medicinal chemistry 2007-05, Vol.15 (10), p.3539-3547
Hauptverfasser:	Shao, Xuan, Gao, Yanfeng, Zhu, Chuanjun, Liu, Xuehui, Yao, Jinlong, Cui, Yuxin, Wang, Rui
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - chemistry Biological and medical sciences Conformation Dimethyl Sulfoxide Endomorphin-2 Enkephalin, Ala-MePhe-Gly- - chemistry Magnetic Resonance Spectroscopy Medical sciences Models, Molecular Molecular Conformation Molecular Mimicry Molecular modeling Neuropharmacology Neurotransmitters. Neurotransmission. Receptors NMR Oligopeptides - chemical synthesis Oligopeptides - chemistry Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems Peptides - chemistry Pharmacology. Drug treatments Phenylalanine - chemistry Receptors, Opioid, mu - drug effects
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