Title of article
Modifications of the 4,4′-residues and sar studies of biphalin, a highly potent opioid receptor active peptide
Author/Authors
Guigen Li، نويسنده , , W. Haq، نويسنده , , Li Xiang، نويسنده , , Bih-Show Lou، نويسنده , , Robert Hughes، نويسنده , , Irene A. De Leon، نويسنده , , Peg Davis، نويسنده , , Terrence J. Gillespie، نويسنده , , Marek Romanowski، نويسنده , , Xiaoyun Zhu، نويسنده , , Aleksandra Misicka، نويسنده , , Andrzej W. Lipkowski، نويسنده , , Frank Porreca، نويسنده , , Thomas P. Davis، نويسنده , , Henry I. Yamamura، نويسنده , , David F. OʹBrien، نويسنده , , Victor J. Hruby، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1998
Pages
6
From page
555
To page
560
Abstract
Modifications of 4,4′ residues of Biphalin have resulted in greater binding selectivity and biological potency for the μ opioid receptor. A higher partition coefficient across the phospholipid bilayer membrane has been achieved by using a β-branched unusual amino acids.
Biphalin, a highly potent antinociceptive peptide, has been modified on 4, 4′ positions by using β-branched and aromatic substituted unusual amino acids. For example: (Tyr-D-Ala-Gly-Phe-NH)2 ------> (Tyr-D-Ala-Gly-(2S,3R)β-Me-Phe-NH)2
Journal title
Bioorganic & Medicinal Chemistry Letters
Serial Year
1998
Journal title
Bioorganic & Medicinal Chemistry Letters
Record number
789280
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