Aqueous solutions of 0.1 M amino acid and 0.1 M trimetaphosphate maintained at chosen pH values between 8.0 and 10.5 and at room temperature in the presence of imidazole or 1,2,4-triazole give rise after a few days to the corresponding peptides. Yields are highest when the pH is adjusted with concentrated NaOH or KOH instead of ammonia; in some cases glycine is quantitatively transformed within 10-15 days into peptides, mainly di-and tripeptides.
Glycine in aqueous solutions of trimetaphosphate or linear polyphosphate at pH adjusted to 8.1‐9.0, is condensed at room temperature to diglycine and very small amounts of triglycine. The addition of imidazole increases the yield of triglycine by a factor of almost 10; supplementary addition of magnesium ion does not increase this effect. On the contrary to what has been observed at pH 11.5‐12.0, the addition of sodium cyanide or cyanamide at pH 8.1‐9.0 diminishes strongly the yield of triglycine and to a lesser degree that of diglycine. The prebiotic significance of the condensation of amino acids in aqueous solutions of polyphosphates in the presence of imidazole is discussed.
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