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Conformation in solution and dynamics of a structurally constrained linear insect kinin pentapeptide analogue
Author(s) -
Moyna Guillermo,
Williams Howard J.,
Nachman Ronald J.,
Scott A. I.
Publication year - 1999
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(19990415)49:5<403::aid-bip6>3.0.co;2-t
Subject(s) - chemistry , pentapeptide repeat , solvation , nuclear magnetic resonance spectroscopy , molecular dynamics , stereochemistry , nuclear overhauser effect , population , spectroscopy , crystallography , computational chemistry , solvent , organic chemistry , peptide , biochemistry , physics , demography , quantum mechanics , sociology
The preferred conformations of the active diuretic insect kinin pentapeptide analogue Phe–Phe–Aib–Trp–Gly–NH 2 were studied using nmr spectroscopy and molecular modeling. Structure sets consistent with rotating frame nuclear Overhauser effect spectroscopy distance constraints obtained by restrained simulated annealing in vacuo indicate a predominant population of a type II β‐turn involving the Phe 1 –Trp 4 region. An equilibrium between this type II and a type I β‐turn formed by residues Phe 2 and Gly 5 was observed in a 5 ns restrained molecular dynamics simulation using the implicit generalized Born solvent accessible surface area (GB/SA) solvation model. When subjected to 500 ps dynamics with explicit water both β‐turn folds were conserved throughout the simulations. The results obtained with implicit and explicit solvation models are compared, and their consistency with the nmr observations is discussed. The behavior of the linear pentapeptide in this study is in agreement with an earlier report on the consensus conformation of the insect kinin active core derived from analysis of cyclic active analogues. © 1999 John Wiley & Sons, Inc. Biopoly 49: 403–413, 1999