Hannes Reiner

Amino acids on the rampant primordial Earth: Electric discharges and the hot salty ocean

For more than 50 years scientists who study prebiotic chemistry have been dealing with chemical evolution as it could have possibly taken place on the primordial Earth. Since we will never know what processes have really taken place around 3.8 to 4 billion years ago we can only come up with plausible reaction pathways that work well in an early Earth scenario as indicated by geochemists. In our work we have investigated the plausibility of one particularly important branch of prebiotic chemistry, the formation of amino acids, by electric discharge in a neutral atmosphere composed of carbon dioxide, nitrogen, and water vapour above liquid water. We have found yields of various amino acids under different temperature conditions, with and without sodium chloride in a simulated primordial lake or ocean within extremely short reaction times compared to the timespan available for prebiotic evolution.

Stereoselective differentiation in the Salt-induced Peptide Formation reaction and its relevance for the origin of life

All living organisms on earth are almost totally made up of biomolecules of only one chiral form. For example, proteins are built almost exclusively of L-amino acids, and sugars are composed of D-saccharides, a fact that is usually referred to as biohomochirality. Its origin is the center of numerous investigations and theories but is not really elucidated yet. The results of experimental investigations of peptide formation in a prebiotically relevant scenario, as described in this paper, give indications on a possible pathway for the synthesis of homochiral L-peptides in the course of the Salt-induced Peptide Formation (SIPF) reaction.

Catalytically Increased Prebiotic Peptide Formation: Ditryptophan, Dilysine, and Diserine

Abstract“Mutual” amino acid catalysis of glycine on the formation of ditryptophan, dilysine, and diserine in the prebiotically relevant Salt-Induced Peptide Formation (SIPF) Reaction was investigated varying the starting concentration and chirality of the educt amino acid, and analyzing the increase of yield resulting from this catalytic effect. Our results show the possibility of an amplified diverse pool of peptides being available for chemical evolution of larger peptides and proteins using also these more complicated amino acids for the evolution of more complex functions in future biochemical cycles and thus for the emergence of life. Catalytic effects are especially high in the case of serine, the most basic amino acid of the three, but are also significant for the other two examples investigated in the present work. Besides that, especially for serine, but also in the case of tryptophan, differences in catalytic yield increase according to the chiral form of the amino acid used could be observed.

Catalytic effects of glycine on prebiotic divaline and diproline formation.

The catalytic effects of the simple amino acid glycine on the formation of diproline and divaline in the prebiotically relevant salt-induced peptide formation (SIPF) reaction was investigated in systems of different amino acid starting concentrations and using the two enantiomeric forms of the respective amino acid. Results show an improved applicability of the SIPF reaction to prebiotic conditions, especially at low amino acid concentrations, as presumably present in a primordial scenario, and indicate excellent conditions and resources for chemical evolution of peptides and proteins on the early earth. For valine, furthermore differences in catalytic yield increase are found indicating a chiral selectivity of the active copper complex of the reaction and showing a connection to previously found enantiomeric differences in complex formation constants with amino acids.