Peptide chain elongation: A possible role of montmorillonite in prebiotic synthesis of protein precursors |
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| Authors: | Juraj Bujdák Katarína Faybíková Artur Eder Yongyos Yongyai Bernd M. Rode |
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| Affiliation: | (1) Institute of Inorganic Chemistry, Slovak Academy of Sciences, 842 36 Bratislava, Slovakia;(2) Department of Inorganic Chemistry, Faculty of Sciences, Comenius University, 842 15 Bratislava, Slovakia;(3) Institute of General, Inorganic and Theoretical Chemistry, University of Innsbruck, Innrain 52a, A-6020 Innsbruck, Austria |
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| Abstract: | Several studies have proven the ability of montmorillonite to catalyse amino acid condensation under assumed prebiotic conditions, simulating wetting-drying cycles. In this work, the oligomerization of short peptides gly2, gly3, gly4 and ala2 on Ca-and Cu-montmorillonite in drying-wetting cycles at 80 °C was studied. The catalytic effect of montmorillonite was found to be much higher than in the case of glycine oligomerization. From gly2 after 3 weeks, 10% oligomers (up to gly6, with gly3 as main products) are formed. Gly3 and gly4 give higher oligomers even after 1 cycle. Ala2 produces both ala3 and ala4, whereas ala does not produce any oligomers under these conditions. Heteroologomerization was observed: ala-gly-gly is formed from ala and gly2. Much higher yields are obtained using Ca-montmorillonite, because copper (II) oxidizes organic molecules. The influence of the reaction mechanism on the preferential oligomerization of oligopeptides is discussed. |
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