PEPTIDE CHAIN ELONGATION: A POSSIBLE ROLE OF MONTMORILLONITE IN PREBIOTIC SYNTHESIS OF PROTEIN PRECURSORS

作者: Juraj Bujdák , Katarína Faybíková , Artur Eder , Yongyos Yongyai , Bernd M. Rode

DOI: 10.1007/BF01581994

关键词:

摘要: Several studies have proven the ability of montmorillonite to catalyse amino acid condensation under assumed prebiotic conditions, simulating wetting-drying cycles. In this work, oligomerization short peptides gly2, gly3, gly4 and ala2 on Ca-and Cu-montmorillonite in drying-wetting cycles at 80 °C was studied. The catalytic effect found be much higher than case glycine oligomerization. From gly2 after 3 weeks, 10% oligomers (up gly6, with gly3 as main products) are formed. Gly3 give even 1 cycle. Ala2 produces both ala3 ala4, whereas ala does not produce any these conditions. Heteroologomerization observed: ala-gly-gly is formed from gly2. Much yields obtained using Ca-montmorillonite, because copper (II) oxidizes organic molecules. influence reaction mechanism preferential oligopeptides discussed.

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