Thermodynamics of peptide bond formation at clay mineral surfaces |
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Authors: | A. W. Flegmann D. Scholefield |
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Affiliation: | (1) School of Biological Sciences, University of Bath, Claverton Down, Bath, England;(2) Present address: Grasslands Research Institute, Hurley, Maidenhead, Berkshire, England |
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Abstract: | Summary The possibility of surface catalysed condensation of unsubstituted amino acids on kaolinite in aqueous systems at elevated temperatures was investigated; no evidence of clay catalysed polycondensation has been found. The thermodynamic feasibility of the hypothetical lysine/dilysine condensation reaction in the temperature-range up to 90° C was evaluated for a range of experimental conditions by the combination of measured free energies of lysine/dilysine cation exchange on kaolinite and on montmorillonite, and free energies for the analogous condensation reaction in homogeneous solution. The results indicate that, in spite of the high selectivity of the clays for the adsorption of cation dimers from dilute solutions, the thermodynamic barrier to the surface condensation of unsubstituted amino acids on clay minerals in aqueous systems up to 90° C is not lower than it is in homogeneous solution. |
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Keywords: | Prebiotic peptide bond formation Clay mineral surfaces Surface condensation |
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