Crystal structure of Alanine‐Copper(II) complex to understand the mechanism of salt induced prebiotic oligomerization of amino acids

Abstract

Oligomerization of amino acid monomers is the vital step in the formation of longer peptides and functional proteins. In spite of continuing efforts towards solving the puzzle of origin of life, the mystery of chemical evolution remains unsolved. Out of various pathways proposed for the formation of peptides under prebiotic conditions, salt induced peptides synthesis presents the most plausible scenario. In attempts to study mechanism of prebiotic oligomerization of amino acid on primitive earth the current study was aimed to determine the crystal structure of intermediate copper amino acid complex and its supra‐molecular assembly. The Structure of the copper alanine complex obtained from SIPF was studied by x‐ray crystallography. The self‐assembling properties of complex into supra‐molecular nanostructures were studied using Field‐emission electron microscopy (FE‐SEM). Results showed the occurrence of racemization of amino acids. This is the first structural study for copper alanine complex formed from prebiotic peptide synthesis pathway. The aggregational properties of intermediate complex showed the formation of rod like crystals and nanospheres. The findings from our study showed the possible mechanism of prebiotic oligomerization of amino acids on the primitive earth towards formation of longer peptides and functional proteins.