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Conformational Analysis of Neuropeptide Y Segments by CD, NMR Spectroscopy and Restrained Molecular Dynamics
Author(s) -
Gurrath Marion,
Bisello Alessandro,
Bottazzo Katia,
Chung ChunWa,
Mammi Stefano,
Peggion Evaristo
Publication year - 1996
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.62
Subject(s) - dipeptide , neuropeptide y receptor , chemistry , molecular mechanics , stereochemistry , amide , molecular dynamics , peptide , nuclear magnetic resonance spectroscopy , residue (chemistry) , molecular model , neuropeptide , receptor , biochemistry , computational chemistry
Neuropeptide Y (NPY), a peptide amide comprising 36 residue has been shown to act as a potent vasoconstrictor. In order to shed light on the structural requirements for the biological activities with respect to the different prerequisites for affinity to the NPY receptor subtypes Y 1 and Y 2 , in the present study the syntheses and conformational analyses of two C‐terminal segments, NPY(18–36) and NPY(13–36), are described. The results obtained by CD measurements, two‐dimensional NMR spectros copy and a conformational refinement of the NMR‐derived structure by molecular mechanics simulations support the findings of previously published structure –activity relationship studies for biologically active and selective compounds. In particular, the α‐helical conformation as well as an appropriate exposure of the side chains of the critical C‐terminal dipeptide within NPY(18–36) are in agreement with the prerequisites proposed for Y 2 receptor binding of that segment.