Conformational studies on gastrin related peptides by high resolution 1H‐n.m.r.
- 1 February 1986
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 27 (2), 145-152
- https://doi.org/10.1111/j.1399-3011.1986.tb01804.x
Abstract
The secondary structures of three gastrin analogs, HCl · H‐Trp‐Nle‐Asp(O‐tBu)‐Phe‐NH2 (tetragastrin), pGlu‐Ala‐Tyr‐Gly‐Trp‐Nle‐Asp‐Phe‐NH2 (octagastrin), and H‐Leu‐(Glu)5‐Ala‐Tyr‐Gly‐Trp‐Nle‐Asp‐Phe‐NH2 (minigastrin) were studied by 1H‐n.m.r. in dimethylsulfoxide and in trifluoroethanol. All three compounds were found to assume a random conformation in the former solvent, while some ordered secondary structure is present in trifluoroethanol even at the tetra‐peptide level. This was shown by temperature studies and solvent titrations. At least four amide protons were found to be solvent shielded in the longer hormone.Keywords
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