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Lam AT, Faragó EP, Owen MC, et al. The effect of oxidative stress on the bursopentin peptide structure: a theoretical study. Phys Chem Chem Phys. 2014;16(20):9602-9doi: 10.1039/c3cp54799j.
Lam, A. T., Faragó, E. P., Owen, M. C., Fiser, B., Jójárt, B., Jensen, S. J., Csizmadia, I. G., & Viskolcz, B. (2014). The effect of oxidative stress on the bursopentin peptide structure: a theoretical study. Physical chemistry chemical physics : PCCP, 16(20), 9602-9. https://doi.org/10.1039/c3cp54799j
Lam, A T, et al. "The effect of oxidative stress on the bursopentin peptide structure: a theoretical study." Physical chemistry chemical physics : PCCP vol. 16,20 (2014): 9602-9. doi: https://doi.org/10.1039/c3cp54799j
Lam AT, Faragó EP, Owen MC, Fiser B, Jójárt B, Jensen SJ, Csizmadia IG, Viskolcz B. The effect of oxidative stress on the bursopentin peptide structure: a theoretical study. Phys Chem Chem Phys. 2014 May 28;16(20):9602-9. doi: 10.1039/c3cp54799j. PMID: 24730022.
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Phys Chem Chem Phys. 2014 May 28;16(20):9602-9. doi: 10.1039/c3cp54799j.

The effect of oxidative stress on the bursopentin peptide structure: a theoretical study.

Physical chemistry chemical physics : PCCP

A T Lam, E P Faragó, M C Owen, B Fiser, B Jójárt, S J K Jensen, I G Csizmadia, B Viskolcz

Affiliations

  1. Department of Chemistry, University of Toronto, 80 St. George St., Toronto, Ontario, CanadaM5S.

PMID: 24730022 DOI: 10.1039/c3cp54799j

Abstract

Bursopentin (BP(5), H-Cys(1)-Lys(2)-Arg(3)-Val(4)-Tyr(5)-OH), found in the bursa Fabricius of the chicken, is a pentapeptide that protects the organism from oxidative stress by reducing the intracellular generation of reactive oxygen species. Hydrogen abstraction, a common oxidative reaction occurring in proteins, often results in the formation of d amino acid residues. To study the effect of this phenomenon on the structure of bursopentin, each of its residues were converted from the l configuration to the d configuration, and the structures of these peptide epimers were compared to that of the wild-type bursopentin. The conformations, secondary structures, compactness and hydrogen bonding of bursopentin were compared to its epimers using molecular dynamics simulations and first principles quantum chemical computations. It was discovered that the repulsion between the side chains of Lys(2) and Arg(3) influenced the conformation of the peptide regardless of the configuration of these residues. Epimerisation of the Val(4) and Tyr(5) caused a reduction in the compactness of bursopentin. In all cases, the occurrence of a turn structure was relatively high, especially when Arg(3) was in the d configuration. Thermodynamic analysis of the epimerisation process showed that the formation of d amino acid residues is favourable.

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