Influence of solvent and configuration of residues at positions 2 and 3 on distance and mobility of pharmacophore groups at positions 1 and 4 in cyclic enkephalin analogues.
The analgesic activity of opioid peptides is mainly connected with their affinity and selectivity for the mu-receptors. The biological activity of cyclic opioid analogues depends on mutual orientation and conformational freedom of aromatic pharmacophore groups at positions 1 and 4. The distance and distance distributions between chromophores at positions 1 [Phe(p-NO(2)), p-nitrophenylalanine] and 4 [Nal, beta-(2-naphthyl)alanine], which constitute an energy donor-acceptor pair, were calculated based on measured fluorescence intensity decays of a donor (Nal). The influence of the solvent and configuration of the residues at position 2 and 3 on donor-acceptor distance distribution and mobility of pharmacophore groups at position 1 and 4 in cyclic enkephalin analogues are discussed.
Malicka
J
J
Faculty of Chemistry, University of Gdańsk, Sobieskiego 1880-952, Poland.
Groth
M
M
Czaplewski
C
C
Karolczak
J
J
Liwo
A
A
Wiczk
W
W
D004745:Enkephalins / Q000138:chemical synthesis / Q000737:chemistry*; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D012997:Solvents; D013050:Spectrometry, Fluorescence
D004745:Enkephalins; D010456:Peptides, Cyclic; D012997:Solvents