Conformational study of the neurotensin and Substance P fragments: Pro-Arg-Arg-Pro and Arg-Pro-Lys-Pro
- 1 July 1983
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 22 (1), 110-118
- https://doi.org/10.1111/j.1399-3011.1983.tb02074.x
Abstract
The conformational behaviour of the basic hydrophilic Pro-Arg-Arg-Pro and Arg-Pro-Lys-Pro peptides, neurotensin (NT) and Substance P fragments, has been taken up by semi-empirical calculations. The presence of two Pro residues prevents these peptides from giving any folded structure (α helix, β turn.). In both peptides the most stable conformations are essentially relative to more or less stretched structures; structures involving one or more residues in a γ turn form are often encountered in Pro-Arg-Arg-Pro peptide while mixed structures involving residues in very different conformations are found for the Arg-Pro-Lys-Pro-peptide. In both peptides, positively charged Lys and Arg side-chains most often point in opposite directions. The Pro-Arg-Arg-Pro peptide is part of the active NT (7–13) fragment where both Arg residues are necessary to the activity. A tentative study shows that the hydrophilic tetrapeptide induces NT (7–13) stretched conformations.Keywords
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