Efficient multi-point interaction between peptide catalysts and amino acid esters in a bilayer vesicular membrane for highly stereoselective hydrolysis reactions

Abstract

The ¹H NMR NOESY spectra of the multi-point interaction between N(N-benzyloxycarbonyl-L-leucyl)-L-histidine-[(Z)-LLeu-L-His] and methyl N-hexanoyl-L-phenylalanate in a N,N-bisdodecyl-N,N-dimethylammonium bromide membrane confirms that the membrane-assisted, hydrophobic interaction between the peptide catalyst and enantiomeric substrates enhances the Stereoselective hydrolysis of p-nitrophenyl N-acetyl (or decanoyl)-L(or D)-phenylalanate with (Z)-L-Leu-L-His (most effective in di-, tri- or tetra-peptide catalysts with an introduced L-histidyl group).