Enantiomer enrichment in early peptides

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Abstract
The two main ordered conformations of polypeptides, the α-helix and the β-sheet, were considered as possible asymmetric supports for stereoselection processes leading to the enrichment in one enantiomer. α-Helices can accomodate residues of both chirality distributed in the same chain, whereas the formation of β-sheets arises from the association of chain segments containing at least seven residues of the same chirality. When the residue composition departs from the racemic mixture, one handedness of the helix is favored, whereas the β-sheet nuclei become predominantly of a unique chirality. Taking into account these observations, processes of enrichment specific for α-and β-structures were envisaged theoretically as well as experimentally.

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