Adsorption of protein and non-protein amino acids on a clay mineral: a possible role of selection in chemical evolution.

Abstract

The adsorption of protein and non-protein amino acids by Na-montmorillonite was studied at pH 3, 7, and 10, in order to determine whether clays could have played a part in selection of protein over non-protein amino acids in prebiotic times. Five pairs of amino acids, containing two to six carbons, were used at a concentration equal to 100% cation exchange capacity of the clay in adsorption experiments. The following pairs of protein and non-protein amino acids were used: glycine and sarcosine, alpha-alanine and beta-alanine, alpha-aminobutyric acid and gamma-aminobutyric acid, valine and norvaline, L-isoleucine and D-alloisoleucine. No selective adsorption of protein amino acids occurred at varying hydrogen ion concentrations. The one difference observed in the adsorption of amino acids in the mixtures was a three- and four-fold greater adsorption of beta- and gamma-amino acids, respectively, than their alpha-amino acid counterparts under acidic and neutral conditions. Strong and weak adsorption of amino acids on the clay were correlated with mechanisms such as cation exchange and hydrogen bonding. The results of this research are significant to understanding the role of clay in chemical evolution because they do not support the role of preferential adsorption of protein over non-protein amino acids by clays.