Identical Primary Sequence but Different Conformations of the Bioactive Regions of Canine CCK-8 and CCK-58

Identical Primary Sequence but Different Conformations of the Bioactive Regions of Canine CCK-8... The C-terminal bioactive regions of CCK-8 and CCK-58 are identical (DY*MGWMDF-NH 2 , Y* denotes a sulfated tyrosine residue), but these peptides have different patterns of bioactivity. Specifically, CCK-58 binds more avidly to the CCK A receptor while CCK-8 is more potent for stimulation of amylase secretion from pancreatic acini. We postulate that these seemingly contradictory observations reflect a stable conformational change in CCK-58 that enhances binding, but diminishes activation of second messenger. We used CD and NMR spectra to evaluate postulated structural differences between CCK-8 and the carboxy-terminus of synthetic CCK-58. The CD spectra indicate the presence of turns in CCK-8 but a mixture of helical and random coil structures for CCK-58. Comparisons of partial NMR chemical shift assignments of CCK-58 and full assignments for CCK-8 also indicate differences in the backbone conformations for these residues. The data support the hypothesis that these peptides have different, stable, carboxy-terminal structures that may influence bioactivity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochemical and Biophysical Research Communications Elsevier

Identical Primary Sequence but Different Conformations of the Bioactive Regions of Canine CCK-8 and CCK-58

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Publisher
Elsevier
Copyright
Copyright © 1999 Academic Press
ISSN
0006-291x
DOI
10.1006/bbrc.1999.1825
pmid
10600515
Publisher site
See Article on Publisher Site

Abstract

The C-terminal bioactive regions of CCK-8 and CCK-58 are identical (DY*MGWMDF-NH 2 , Y* denotes a sulfated tyrosine residue), but these peptides have different patterns of bioactivity. Specifically, CCK-58 binds more avidly to the CCK A receptor while CCK-8 is more potent for stimulation of amylase secretion from pancreatic acini. We postulate that these seemingly contradictory observations reflect a stable conformational change in CCK-58 that enhances binding, but diminishes activation of second messenger. We used CD and NMR spectra to evaluate postulated structural differences between CCK-8 and the carboxy-terminus of synthetic CCK-58. The CD spectra indicate the presence of turns in CCK-8 but a mixture of helical and random coil structures for CCK-58. Comparisons of partial NMR chemical shift assignments of CCK-58 and full assignments for CCK-8 also indicate differences in the backbone conformations for these residues. The data support the hypothesis that these peptides have different, stable, carboxy-terminal structures that may influence bioactivity.

Journal

Biochemical and Biophysical Research CommunicationsElsevier

Published: Dec 20, 1999

References

  • Biopolymers
    Fournie-Zaluski, M.C.; Durieux, C.; Lux, B.; Belleney, J.; Pham, P.; Gerard, D.; Roques, B.P.
  • Gastroenterology
    Hoffmann, P.; Eberlein, G.A.; Reeve, J.; Bunte, R.H.; Grandt, D.; Goebell, H.; Eysselein, V.E.

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