151965-03-6Relevant articles and documents
Conformational perturbations induced by N-amination and N-hydroxylation of peptides
Dupont, Virginie,Lecoq, Alain,Mangeot, Jean-Paul,Aubry, André,Boussard, Guy,Marraud, Michel
, p. 8898 - 8906 (1993)
Amination and bydroxylation of the amide nitrogen in a peptide chain have little influence on the local geometry, but both affect the hydrogen-bonding network, and therefore the conformational properties of the modified peptide. An experimental study in solution (IR spectroscopy and 1H-NMR) and in the solid state (X-ray diffraction) has been carried out on the N-amino and N-hydroxy analogues of the two RCO-Pro-NHMe and RCO-Pro-Gly-NHiPr peptides known to adopt preferentially the γ- and β-turn structures, respectively. The N-amino group is a weak proton donor which does not interact significantly with the peptide chain. On the contrary, the N-hydroxyl group is a strong proton donor giving close contacts with the peptide carbonyls. The resulting folded conformers of an expanded γ- or β-like type, presenting an 8- or 11-membered cycle instead of a 7- or 10-membered cycle in the cognate peptides have been also analyzed by a SYBYL molecular dynamics simulation.
