The role of the peptides at the origin of life
From MaRDI portal
(Redirected from Publication:1704342)
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.
Recommendations
- The first peptides: the evolutionary transition between prebiotic amino acids and early proteins
- Lipid domain boundaries as prebiotic catalysts of peptide bond formation
- The kinetics of the growth of an accidentally created chiral biomolecule in the racemic prebiotic medium
- Ionic and chiral asymmetries as physical factors of biogenesis and ontogenesis
- Chiral symmetry breaking: Frank model for the evolution of homochirality described by population dynamics
Cited in
(2)
This page was built for publication: The role of the peptides at the origin of life
Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q1704342)
