β-structures of polypeptides with L- and D-residues

Summary

It was previously shown that nuclei ofβ-sheets surrounded by unordered segments are formed in polypeptide chains built up with alternating hydrophobic and hydrophilic residues and containing both L- and D-enantiomers. It was also established that segments of residues having the same configuration tend to segregate in these nuclei when the starting composition of stereomonomers departs from the racemic mixture.

Soft acidic hydrolysis of these polymers has been studied. Kinetic measurements show two pseudo first order rate constants, in agreement with the existence of two conformational species. The unordered part of the chains is hydrolyzed more rapidly, allowing the isolation of aβ-fraction enriched in one enantiomer. Thus, a plausible process of enrichment in enantiomer during prebiotic evolution has been described, which however does not explain the preference of one enantiomer over the other one.