Conformational analysis of the simplest chiral pseudo-peptide and selected derivatives

I. V. Repyakh, E. Deretey, I. G. Csizmadia

Research output: Contribution to journalArticle

1 Citation (Scopus)


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 results, it follows that in general pseudo-peptides can mimic the backbone of the parent peptides. These computational results are in full agreement with previously reported experimental data. N-formyl pseudo-alanine was shown to be more flexible, than the parent peptide. (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)81-96
Number of pages16
JournalJournal of Molecular Structure: THEOCHEM
Issue number1-2
Publication statusPublished - May 9 2000


  • Pseudo-peptide
  • Semi-empirical and ab initio MO calculations

ASJC Scopus subject areas

  • Biochemistry
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

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