Abstract:
:Opioid receptor analyses of deltorphin A (H-Tyr-D-Met-Phe-His-Leu-Met-Asp-NH2) analogues indicated the following: (a) increased negativity differentially affected affinities (Ki) and selectivity (Ki mu/Ki delta); (b) shifted sequence heptapeptides, [Asp5,Leu6,Met-NH2(7)] and [Asp4,His5,Leu6,Met-NH2(7)], reversed selectivity (delta-->mu); (c) substitutions at positions 4, 5, and 6 diminished selectivity, with changes in residue 5 being the most detrimental; (d) C-terminal deletions differentially effected Ki. These are the first data to demonstrate a reversal of delta selectivity in heptapeptides containing a negative charge and indicate that modifications in affinity occur through changes in both anionic and hydrophobic properties of residues at specific positions in the peptide. Deltorphin analogues might also be applied to differentiate between opioid receptor subsites.
journal_name
Peptidesjournal_title
Peptidesauthors
Lazarus LH,Salvadori S,Attila M,Grieco P,Bundy DM,Wilson WE,Tomatis Rdoi
10.1016/0196-9781(93)90006-3subject
Has Abstractpub_date
1993-01-01 00:00:00pages
21-8issue
1eissn
0196-9781issn
1873-5169pii
0196-9781(93)90006-3journal_volume
14pub_type
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