The role of the peptides at the origin of life

DOI10.1016/J.JTBI.2017.06.023zbMATH Open1382.92135arXiv1702.01623OpenAlexW2660499424WikidataQ47993824 ScholiaQ47993824MaRDI QIDQ1704342FDOQ1704342

Authors: Soren Toxvaerd 

Publication date: 9 March 2018

Published in: Journal of Theoretical Biology (Search for Journal in Brave)

Abstract: The peptides in biosystems are homochiral polymers of L-amino acids, but razemisate slowly by an active isomerization kinetics. The chemical reactions in biosystems are, however, reversible and what racemisates the peptides at the water activity in the biosystems can ensure homochirality at a smaller activity. Here we show by a thermodynamics analysis and by comprehensive Molecular Dynamics simulations of models of peptides, that the isomerization kinetics racemisates the peptides at a high water activity in agreement with experimental observations of aging of peptides , but enhances homochirality at a smaller water activity. The hydrophobic core of the peptide in an enzyme can ensure homochirality at a low water activity, and thus the establishment of homochirality at the origin of life and ageing of peptides and dead of biosystems might be strongly connected.

Full work available at URL: https://arxiv.org/abs/1702.01623

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zbMATH Keywords

simulationsisomerizationhomochirality

Mathematics Subject Classification ID

Biochemistry, molecular biology (92C40) Problems related to evolution (92D15) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

Cites Work

• RNA secondary structures and their prediction

Cited In (2)

• Lipid domain boundaries as prebiotic catalysts of peptide bond formation
• The first peptides: the evolutionary transition between prebiotic amino acids and early proteins

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