Conformational analysis of the simplest chiral pseudo-peptide and selectedderivatives

Citation
Iv. Repyakh et al., Conformational analysis of the simplest chiral pseudo-peptide and selectedderivatives, J MOL ST-TH, 503(1-2), 2000, pp. 81-96
Citations number
15
Categorie Soggetti
Physical Chemistry/Chemical Physics
Journal title
JOURNAL OF MOLECULAR STRUCTURE-THEOCHEM
ISSN journal
01661280 → ACNP
Volume
503
Issue
1-2
Year of publication
2000
Pages
81 - 96
Database
ISI
SICI code
0166-1280(20000509)503:1-2<81:CAOTSC>2.0.ZU;2-K
Abstract
Conformational properties of three model pseudo-peptides were investigated by semi-empirical and ab initio MO methods. The three simplest model pseudo -peptides included the protonated form of N-formyl pseudo-alanineamid HCONH -CHMe-CH2NH3+, N-formyl pseudo-alanine itself HCONH-CHMe-CH2NH2. as well as the formylated N-formyl pseudo-alanine (i.e. propylene-di(N-formylamine)) HCONH-CHMe-CH2NHCOH. It was shown that geometries of the pseudo-peptides in their global minima were determined by H-bonds. From the computated result s, it follows that in general pseudo-peptides can mimic the backbone of the parent peptides. These computational results are in full agreement with pr eviously reported experimental data. N-formyl pseudo-alanine was shown to b e more flexible, than the parent peptide. (C) 2000 Elsevier Science B.V. Al l rights reserved.