Chiral recognition of dipeptides in bio-membrane models: the role of amphiphile hydrophobic chains

The influence of the hydrophobic chain length on the chiral recognition capabilities of sodium N-acylprolinate micellar aggregates, used as biomembrane models, was investigated by 1H NMR on the enantiomer couples of ditryptophan. The length of the hydrophobic portion of the surfactant is shown to influence the mode of enantiodiscrimination. Interestingly the hydrophobic chain length also affects the site of binding of heterochiral enantiomers as well as their conformation inside the aggregates. © 2007 Elsevier Ltd. All rights reserved