Synthesis of a new group of deltorphin I/II analogs modified in the address domain with gamma-amino acids, and QSAR study of their delta/mu opioid binding
The delta selectivity of the opioid heptapeptides deltorphin I and II has been attributed to the C-terminal "address" domain, the hydrophobic Val(5)-Val(6) residues apparently playing a topographical role. We now report the synthesis, opioid binding affinities, and a QSAR study of a series of peptides in which these valine residues were replaced with gamma-amino acids. Results support a conformation stabilization role for this domain, rather than interaction with a receptor binding pocket.
Heyl, D. L., Sanvordekar, M. D., Dogruyol, G., Salamoun, M. D., Rodgers, D. W., Renganathan, K., … Schullery, S. E. (1999). Synthesis of a new group of deltorphin I/II analogs modified in the address domain with gamma-amino acids, and QSAR study of their delta/mu opioid binding. Protein and Peptide Letters, 6(6), 359–366.
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