Enhanced in vivo activity of peptidase-resistant analogs of the insect kinin neuropeptide family

The diuretic/myotropic insect kinin neuropeptides, which share the common C-terminal pentapeptide core FX 1X 2WG-NH 2, reveal primary (X 2-W) and secondary (N-terminal to F) sites of susceptibility to peptidases bound to corn earworm ( H. zea) Malpighian tubule tissue. Analogs designed to enhance re...

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Veröffentlicht in:	Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2002-04, Vol.23 (4), p.735-745
Hauptverfasser:	Nachman, Ronald J., Strey, Allison, Isaac, Elwyn, Pryor, Nan, Lopez, Juan D., Deng, Jin-Gen, Coast, Geoffrey M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Diuresis Insect Proteins - chemistry Insect Proteins - metabolism Insect Proteins - pharmacology Insecta - metabolism kinin Kinins - chemistry Kinins - metabolism Kinins - pharmacology Male Malpighian Tubules - drug effects Malpighian Tubules - metabolism Neuropeptides - chemistry Neuropeptides - metabolism Neuropeptides - pharmacology peptidase Peptide Hydrolases - metabolism
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