Conformational and biological properties of the Ala10-analog of human Des-Trp1, Nle12-minigastrin

• Published in: Biochemistry (Easton) Vol. 28; no. 18; pp. 7182 - 7188
• Main Authors: Mammi, Stefano, Foffani, Maria Teresa, Peggion, Evaristo, Galleyrand, Jean Claude, Bali, Jean Pierre, Simonetti, Mario, Goehring, Walter, Moroder, Luis, Wuensch, Erich
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 05.09.1989
• Subjects: Alanine; Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chemical Phenomena; Chemistry; Circular Dichroism; Fundamental and applied biological sciences. Psychology; Gastric Acid - metabolism; Gastrins - analysis; Gastrins - biosynthesis; Gastrins - metabolism; Gastrins - pharmacology; Humans; Magnetic Resonance Spectroscopy; Male; Protein Binding; Protein Conformation; Proteins; Rabbits; Rats; Temperature; Human; Analysis; Circular dichroism spectrometry; Gastrin; Peptide hormone; HPLC chromatography; Biosynthesis; NMR spectrometry; Biological activity; Conformation

Synthesis, conformation, and biological properties of the Ala10 analogue of des-Trp1,Nle12-minigastrin are reported. Replacement of the Gly residue in the original sequence with Ala remarkably changes the conformational preference of the hormone in trifluoroethanol. CD and NMR results indicate that...