The taste of D- and L-amino acids: In vitro binding assays with cloned human bitter (TAS2Rs) and sweet (TAS1R2/TAS1R3) receptors.

The taste of different enantiomeric forms of amino acids has been deeply investigated because it represents the most impressive case of correlation between stereochemistry and flavour. Herein, we aimed to elucidate the molecular activity of d- and l-amino acids using an in vitro system based on a cellular model overexpressing sweet and bitter receptors, and to analyse the correlation between in vitro and sensory studies. With our work we demonstrated specific enantiomeric activities for several amino acids on TAS1R2-TAS1R3 sweet receptor. Moreover, we proved interaction of tryptophan and phenylalanine with a specific group of TAS2Rs bitter receptors, confirming and improving the results recently obtained in the tasting of amino acids. In addition, we provide the first systematic analysis of l- and d-amino acid actions on the sweet heterodimeric receptor.