Stationary Points on the PES of N-Methoxy Peptides and Their Boron Isosteres: An Ab Initio Study

Malde, Alpeshkumar K., Khedkar, Santosh A. and Coutinho, Evans C. (2006) Stationary Points on the PES of N-Methoxy Peptides and Their Boron Isosteres: An Ab Initio Study. Journal of Chemical Theory and Computation, 2 6: 1664-1674. doi:10.1021/ct600192g

Author Malde, Alpeshkumar K.
Khedkar, Santosh A.
Coutinho, Evans C.
Title Stationary Points on the PES of N-Methoxy Peptides and Their Boron Isosteres: An Ab Initio Study
Journal name Journal of Chemical Theory and Computation   Check publisher's open access policy
ISSN 1549-9618
Publication date 2006-01-01
Year available 2006
Sub-type Article (original research)
DOI 10.1021/ct600192g
Open Access Status
Volume 2
Issue 6
Start page 1664
End page 1674
Total pages 11
Place of publication Washington, D.C.
Publisher American Chemical Society
Language eng
Subject 030701 Quantum Chemistry
Abstract The conformational space of N-methoxy-N-methylacetamide [CH3−CO−N(OCH3)CH3, NMA-NOM] and its boron isostere [CH3−CO−B(OCH3)CH3, BMA-BOM] has been studied at the HF, B3LYP, and MP2 levels of theory with the 6-31+G* basis set. The minima, saddle points, and rotation barriers on the PES of these molecules have been located, and the energy barriers estimated. The omega rotation barrier is relatively lower in the boron isostere than in NMA-NOM. The difference in the rotation barrier has been attributed to second-order orbital interactions, like negative hyperconjugation, as revealed by NBO calculations. As an extension, N-acetyl-N‘-methoxy-N‘-methylamide of alanine (Ala-NOM) and its boron isostere (B-Ala-BOM) have been adopted as model peptides to study the conformational preferences about the phi and ψ torsion angles. The study reveals a strong preference for conformations of type-V beta turn and left-handed α-helix for Ala-NOM. B-Ala-BOM, on the other hand, favors conformations of type-Va beta turn, mirror image of Poly-L-Pro II helix, and structures with positive phi and extended ψ. The replacement of nitrogen by boron changes the electronic and conformational properties of the peptide, extends greater flexibility around the omega angle, induces a strong preference for positive phi values, and shifts the site of nucleophilic attack from the carbonyl group to boron.
Keyword Chemistry, Physical
Physics, Atomic, Molecular & Chemical
Q-Index Code C1
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
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