Paper Info
Title
Computational study of conformational preferences of thioamide-containing azaglycine peptides.
Abstract
The effect of thioamide substitution on the conformational stability of an azaglycine-containing peptide, For-AzaGly-NH2 (1), was investigated for the sake of finding possible applications by using ab initio and DFT methods. As model compounds, For-[PsiCSNH]-AzaGly-NH2 (2), For-AzaGly-[PsiCSNH]-NH2 (3), and For-[PsiCSNH]-AzaGly-[PsiCSNH]-NH2 (4) were used. Two-dimensional phi-psi potential energy surfaces (PESs) for 2-4 were calculated at the B3LYP/6-31G*//HF/6-31G* level in gas (epsilon = 1.0) and in water (epsilon = 78.4) by applying the isodensity polarizable continuum model (IPCM) method. On the basis of these PESs, the minimum energy conformations for 2-4 were characterized at the B3LYP level with 6-31G*, 6-311G**, and 6-31+G** basis sets. The remarkable structural effect of thioamide substitution for 2-4 is that beta-strand structure is observed as a global or local minimum. The minima of 2-4 are also compared with those for glycine and thioamide-containing glycine peptides. Our theoretical results demonstrate that compounds 2-4 would be used to design controllable secondary structures. (C) 2003 Wiley Periodicals, Inc.
Year
DOI
Venue
2004
10.1002/jcc.10364
JOURNAL OF COMPUTATIONAL CHEMISTRY
Keywords
Field
DocType
peptidomimetics,azapeptide,thioamide,beta-strand,DFT method
Polarizable continuum model,Peptide,Computational chemistry,Chemistry,Maxima and minima,Potential energy,Peptidomimetic,Ab initio,Thioamide
Journal
Volume
Issue
ISSN
25
2
0192-8651
Citations 
PageRank 
References 
0
0.34
0
Authors
7
Name
Order
Citations
PageRank
Ho-Jin Lee120040.97
Jong Hyun Kim27716.14
Hee Jung Jung350.84
Kun-Young Kim400.34
Eun Jung Kim587367.64
Youngsang Choi671.86
Chang-Ju Yoon700.34