Peptide chain elongation: a possible role of montmorillonite in prebiotic synthesis of protein precursors.
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 degrees 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.
Bujdák
J
J
Institute of Inorganic Chemistry, Slovak Academy of Sciences, Bratislava.
Faybíková
K
K
Eder
A
A
Yongyai
Y
Y
Rode
B M
BM
D000409:Alanine / Q000737:chemistry*; D001546:Bentonite / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry*; D010441:Peptide Chain Elongation, Translational; D010455:Peptides / Q000138:chemical synthesis*
D010455:Peptides; D001546:Bentonite; D000409:Alanine; D005998:Glycine