1H-n.m.r. investigation of conformational features of cyclic, penicillamine-containing enkephalin analogs.
Conformational features of a series of cyclic, penicillamine-containing enkephalin analogs, all of which display selectivity for the delta opioid receptor, were studied by 1H n.m.r. in aqueous solution. Comparison of chemical shifts, coupling constants, and temperature dependence of amide proton chemical shifts suggests different conformational features among the analogs, some of which can be related to the different primary sequences of these peptides. The observation that some of the analogs display disparate individual conformational features while exhibiting similar opioid potency and receptor selectivity suggests that such analogs may share a similar overall topography or at the least maintain the same relative orientations of key portions of the molecule.
D020881:Enkephalin, D-Penicillamine (2,5)-; D004745:Enkephalins / Q000138:chemical synthesis; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D004745:Enkephalins; C040242:enkephalin, Cys(2)-Pen(5)-; C038233:enkephalin, Pen(2)-Cys(5)-; D020881:Enkephalin, D-Penicillamine (2,5)-