Enantioselective recognition of histidine and lysine esters by porphyrin chiral clefts and detection of amino acid conformations in the bound state

Maxwell J. Crossley*, Lindsey G. MacKay, Andrew C. Try

*Corresponding author for this work

Research output: Contribution to journalArticle

137 Citations (Scopus)

Abstract

Resolution of the bisporphyrin Tröger's base analogue 1 affords homochiral clefts that tightly bind histidine esters in 80-86% e.e. and lysine benzyl ester in 48% e.e.; the histidine esters are bound in fixed conformations that can be readily detected by 1H NMR spectroscopy as a result of the large dispersion of proton resonances by the ring currents of the two porphyrins.

Original languageEnglish
Pages (from-to)1925-1927
Number of pages3
JournalJournal of the Chemical Society, Chemical Communications
Issue number18
DOIs
Publication statusPublished - 1995

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