Cited by 57Origins and Evolution of LifeRNA and protein synthesis mechanismsSpace Science and Extraterrestrial Life

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

Peptide Synthesis in Early Earth Hydrothermal Systems

Abstract

We report here results from experiments and thermodynamic calculations that demonstrate a rapid, temperature-enhanced synthesis of oligopeptides from the condensation of aqueous glycine. Experiments were conducted in custom-made hydrothermal reactors, and organic compounds were characterized with ultraviolet-visible procedures. A comparison of peptide yields at 260 degrees C with those obtained at more moderate temperatures (160 degrees C) gives evidence of a significant (13 kJ . mol(-1)) exergonic shift. In contrast to previous hydrothermal studies, we demonstrate that peptide synthesis is favored in hydrothermal fluids and that rates of peptide hydrolysis are controlled by the stability of the parent amino acid, with a critical dependence on reactor surface composition. From our study, we predict that rapid recycling of product peptides from cool into near-supercritical fluids in mid-ocean ridge hydrothermal systems will enhance peptide chain elongation. It is anticipated that the abundant hydrothermal systems on early Earth could have provided a substantial source of biomolecules required for the origin of life.

Overview

Integrity signals

Registry

Crossref · 10.1089/ast.2008.0166

Cites

34 of 34 references verified0 citation errors · 0 not checkable

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  • The selection mechanism is especially high for peptides formed from racemic amino acids under hydrothermal conditions, and the selection effect may be stronger for peptides that are amphiphilic and reflect the spatial distribution of hydrophilicity and hydrophobicity of the bilayer membrane.

    “The potential of this selection mechanism is especially high in the case of peptides which are being formed from racemic amino acids under hydrothermal conditions [24]. The selectivity for hydrophobic peptides has already gained early recognition [22]. However, the selection effect may even be stronger for those peptides which, with a suitable composition and sequence of amino acids, are amphiph”

    From Selection of Prebiotic Molecules in Amphiphilic Environments (2017) · cites this paper as [24]

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Research works printed but not linked: 3

  1. Martin R.B., 2001, Met. Ions Biol. Syst., 38, 1
  2. Rosenbauer R.J., 1993, American Mineralogist, 78, 1286
  3. 10.2113/100.3.419 · DOI

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Metadata

Authors
Lemke, K. H., Rosenbauer, R. J., & Bird, D. K.
Affiliations
  • United States Geological Survey (US)
  • Stanford University (US)
Venue
Astrobiology
Published
2009-03
Volume
9
Issue
2
Pages
141-146
ISSN
  • 1531-1074 (ISSN-L)
  • 1557-8070
OpenAlex
W2027622373
Cited by
56
References
34
Citations by year
2026: 3 · 2025: 3 · 2024: 1 · 2023: 2 · 2022: 3 · 2021: 3 · 2020: 5 · 2019: 6 · 2018: 6 · 2017: 4 · 2016: 4 · 2015: 3 · 2014: 8 · 2013: 1 · 2012: 1
FWCI
0.67
Type
journal article
Language
en
Open access
closed
Locations
  • Astrobiology (publishedVersion)
  • PubMed (publishedVersion)
  • The HKU Scholars Hub (University of Hong Kong) (submittedVersion)
Topics
  • Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Space Science and Extraterrestrial Life
Keywords
peptide synthesis, hydrothermal systems, early Earth, origin of life, oligopeptides, exergonic reactions, peptide hydrolysis, amino acid stability, mid-ocean ridge hydrothermal systems
MeSH terms
Origin of Life, Atmospheric Pressure, Buffers, Chromatography, High Pressure Liquid, Glycine, Hot Temperature, Hydrogen-Ion Concentration, Peptide Biosynthesis, Phosphates, Seawater, Spectrophotometry, Ultraviolet, Thermodynamics, Time Factors, Water, Evolution, Chemical

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