Abstract
Analysis of possible μ opioid receptor active conformations for dermorphin suggested that the topographical location of the tyramine moiety of the N-tenninal tyrosine can be simulated with the phenol of tyrosine1 or desamino-tyrosine1 (4-hydroxyphenylpropionic acid) and a basic group located on the side chain of a dibasic acid residue located in position 2. The biological properties of respective analogs with D- or L-arginine, and D- or L-lysine in the position 2 of dermorphin or desaminodermorphin and their N-terminal tetrapeptide fragments, has provided evidence in support of this prediction, and questions the dogma that an N-terminal tyrosine is a necessary element for opioid agonist peptides.
Original language | English (US) |
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Pages (from-to) | 1633-1640 |
Number of pages | 8 |
Journal | Life Sciences |
Volume | 57 |
Issue number | 18 |
DOIs | |
State | Published - Sep 22 1995 |
Keywords
- GPI assay
- MVD assay
- binding assays
- dermorphin analogues
- dibasic amino acids
- δ opioid receptor
- μ opioid receptor
ASJC Scopus subject areas
- General Pharmacology, Toxicology and Pharmaceutics
- General Biochemistry, Genetics and Molecular Biology