Add time:08/16/2019 Source:sciencedirect.com
The mechanism of the thermal polymerization (at 180°C) of glutamic acid, tyrosine, and glycine has been studied. Glutamic acid is quickly and almost completely converted into pyroglutamic acid. The only dipeptide that is formed by dimerization of the remaining two amino acids is cyclic glycyl-tyrosine (a diketopiperazin). In a secondary reaction pyroglutamic acid interacts with cyclic glycyl-tyrosine and yields pyroglutamyl-glycyltyrosine and pyroglutamyl-tyrosyl-glycine. Other di- or tripeptides are not observed. The preferential appearance of the two pyroglutamyl-peptides has been reported earlier by Nakashima et al. (1977). The present data explain those results. Model experiments show that cyclic glycyl-tyrosine can also be cleaved by other acids or bases. In the presence of acetic acid at 118°C N-acetyl-glycyl-tyrosine is the major product. Partial hydrolysis predominantly yields tyrosyl-glycine. These effects are explained by stereospecific interactions. The results on self-ordering of amino acids during peptide formation are discussed in respect of the origin of prebiotic enzymes and genetic information.
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