Impairment of a model peptide by oxidative stress: Thermodynamic stabilities of asparagine diamide Cα-radical foldamers

Klára Z. Gerlei, Lilla Élo, Béla Fiser, Michael C. Owen, Imre Jákli, Svend J. Knak Jensen, Imre G. Csizmadia, András Perczel, Béla Viskolcz

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Abstract

Electron structure calculations on N-acetyl asparagine N-methylamide were performed to identify the global minimum from which radicals were formed after H-abstraction by the OH radical. It was found that the radical generated by breaking the C-H bond of the α-carbon was thermodynamically the most stable one in the gas- and aqueous phases. The extended (βL and βD) backbone conformations are the most stable, but syn-syn or inverse γ-turn (γL) and γ-turn (γ D) have substantial stability too. The highest energy conformers are the degenerate εL and εD foldamers. Clearly, the most stable β foldamer is the most likely intermediate for racemization.

Original languageEnglish
Pages (from-to)104-108
Number of pages5
JournalChemical Physics Letters
Volume593
DOIs
Publication statusPublished - Feb 11 2014

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ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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