Structure-taste relationships of aspartyl tripeptide esters.
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A series of twenty four analogues of L-α–Asp–Gly–Gly–OMe has been synthesized in relation to structural features of sweet peptides. The rule in the structure-taste relationships of dipeptides is held in the sweet aspartyl tripeptide esters. In order for the aspartyl tripeptide esters to be sweet, the second amino acid must have a D-configuration and a small, compact alkyl group (Me, Et, or <I>i</I>-Pr) at R<SUP>2</SUP>. An L-configuration of the third amino acid is required for a potent sweet taste. It has been concluded that the small alkyl group at R<SUP>2</SUP> participates in binding with the receptor through a hydrophobic interaction and increases the sweetness potency.
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