Structural and biochemical studies of human galanin: NMR evidence for nascent helical structures in aqueous solution

Biochemistry
M B MorrisT P Iismaa

Abstract

The 30-residue human neuropeptide, galanin, was shown to bind to rat insulinoma RINm5F cells and to inhibit glyceraldehyde-stimulated insulin secretion from these cells in a manner quantitatively similar to that of porcine galanin. Neither human nor porcine galanin stimulated Ca2+ mobilization in cultured human small cell lung carcinoma cells. Sedimentation equilibrium analysis of human galanin showed that it was strictly monomeric in aqueous solution, indicating that the peptide interacts with its receptor(s) as a monomer. The monomeric nature of the peptide makes it especially suitable for structural studies using NMR. Nuclear Overhauser enhancement spectroscopy experiments performed on galanin dissolved in aqueous solution (150 mM KCl, pH 4) at both 33 and 3 degrees C indicate that certain regions of the peptide are capable of adopting detectable levels of short-range structure in rapid equilibrium with random coil. At 33 degrees C, the short-range structures include a nascent helix spanning residues 3-11 which incorporates a hydrophobic core from residues 6-11. Residues 14-18 and 22-30 display sequential NH-NH and C beta H-NH connectivities, indicating that these regions of the peptide adopt nonrandom conformations by signi...Continue Reading

Citations

Feb 9, 1996·Journal of Chromatography. B, Biomedical Applications·T JanákyB Penke
Jun 10, 2005·Neuropeptides·Linda LundströmTamas Bartfai
Dec 15, 2012·Molecular Membrane Biology·Wiktor JurkowskiArne Elofsson
Aug 13, 2002·The Journal of Biological Chemistry·Sharon Wald KraussJoel Anne Chasis

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