Some aspects of the relationship between the structure of a bitter diketopiperazine and its receptor

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Abstract
A conformation of a diketopiperazine, cyclo(L‐leucyl‐L‐tryptophyl), was determined by nmr and x‐ray analysis. The receptor for this bitter diketopiperazine neither recognizes chirality nor requires a strict conformation of the substrate. A good correlation was found between the bitterness of diketopiperazine and its hydrophobicity. Experiments using liposome as a model of the receptor membrane suggested that a lecithin‐like lipid is a candidate for a binding site of the bitter diketopiperazine. Furthermore, affinity chromatography using cyclo(L‐leucyl‐L‐phenylalanyl) as a bitter ligand indicated that phosphoglycerides of the lipids tested showed a particular affinity to the bitter diketopiperazine.

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