Modifications of the 4,4'-residues and SAR studies of Biphalin, a highly potent opioid receptor active peptide.
Modifications of 4,4' residues of Biphalin have resulted in greater binding selectivity and biological potency for the mu opioid receptor. A higher partition coefficient across the phospholipid bilayer membrane has been achieved by using a beta-branched unusual amino acids.
Li
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G
Department of Chemistry, University of Arizona, Tucson 85721, USA.
Haq
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Xiang
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Lou
B S
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Hughes
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De Leon
I A
IA
Davis
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Gillespie
T J
TJ
Romanowski
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M
Zhu
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X
Misicka
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A
Lipkowski
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Porreca
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F
Davis
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Yamamura
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O'Brien
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Hruby
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D000700:Analgesics / Q000737:chemistry* / Q000494:pharmacology; D000818:Animals; D004745:Enkephalins / Q000737:chemistry* / Q000494:pharmacology; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008051:Lipid Bilayers; D017450:Receptors, Opioid, mu / Q000187:drug effects*; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D000700:Analgesics; D004745:Enkephalins; D008051:Lipid Bilayers; D017450:Receptors, Opioid, mu; C053673:biphalin