Macrocyclic receptors for carboxylate termini of amino acids and peptides

Gale, Nittaya (2004) Macrocyclic receptors for carboxylate termini of amino acids and peptides. University of Southampton, Doctoral Thesis.

Abstract

This thesis describes the synthesis of macrobicyclic receptors designed to bind N-protected amino acid and dipeptide guests by hydrogen bond formation from thiourea or guanidinium groups in the hosts to the carboxylate terminus of the guests and by other interactions from four amide functional groups at the rim of bowl-like macrobicycles and/or from the lone pair of nitrogen atoms in the pyridine rings present in some of the hosts.  The first chapter discusses supramolecular chemistry and previous work in this area.

The second chapter describes the synthesis of macrobicycles containing bis-thioureas as the carboxy binding sites (CBS), linked via lysine derivatives to a rigid rim consisting of four aromatic rings and four amide bonds.  The binding properties of these macrocycles are investigated using N-protected glutamate and aspartate salts and a variety of mono-carboxylates.  The protected aspartate and glutamate were found to bind in multiple binding modes to these receptors.

The third chapter describes the synthesis of macrocycles containing a single thiourea or guanidinium group with extra NH groups at the CBS and glutamic acid derived side walls.  These receptors were designed to bind dipeptides containing a single carboxylate group such as alanylalanine.  These receptors were found to bind L,L-isomers more strongly than D,D-isomers by up to seven times.

The fourth chapter describes the synthesis of water-soluble macrobicycles containing two lysine groups.  These systems were found to bind alanylalanine in DMSO.

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