4.6 Article

Effect of condensation agents and minerals for oligopeptide formation under mild and hydrothermal conditions in related to chemical evolution of proteins

Journal

ADVANCES IN SPACE RESEARCH
Volume 44, Issue 2, Pages 267-275

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.asr.2009.03.027

Keywords

Prebiotic chemistry; Peptide; Hydrothermal system; Amino acid; Primitive Earth; Origin of life in space

Funding

  1. Japan Society for the Promotion of Science (JSPS) [20540476]
  2. Grants-in-Aid for Scientific Research [20540476] Funding Source: KAKEN

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The role of condensation agents and minerals for oligopeptide formation was inspected to see whether minerals possess catalytic activity under mild and hydrothermal conditions. Under mild conditions, oligopeptide formation from negatively charged amino acids (Asp and Glu) using different minerals and the elongation of alanine oligopeptides ((Ala)(2)-(Ala)(5)) were attempted using apatite minerals. Oligo(Asp) up to 10 amino acid units from Asp were observed in the presence of 1-ethyl-3-(3-dimethylaminopropyl carbodiimide (EDC). Notable influence of minerals was not detected for the oligo(Asp) formation. Oligo(Asp) was gradually degraded by the further incubation in the presence of EDC in both the absence and presence of minerals. The formation of oligo(Glu) was less efficient in the presence of carbonyldiimidazole. The elongation from (Ala)(3), (Ala)(4), and (Ala)(5) and the formation of diketopiperazille from (Ala)(2) proceeded immediately in the presence of EDC in the meantime of the sample preparations. In addition, it was unexpected that the disappearance of the products and the reformation of the reactants occurred by the further incubation for 24 h; for instance, (Ala)(5) decreased but (Ala)(4) increased with increasing the reaction time in the reaction of (Ala)(4) with EDC. These facts suggest that the activation of the reactant amino acids or peptides immediately occurs. Under the simulated hydrothermal conditions, EDC did not enhance the formation of oligopeptides from Asp, Glu or Ala nor the spontaneous formation of (Ala)(5) from (Ala)(4). (C) 2009 COSPAR. Published by Elsevier Ltd. All rights reserved.

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