BMC Structural Biology 2007-11-01

The binding site for neohesperidin dihydrochalcone at the human sweet taste receptor.

Marcel Winnig, Bernd Bufe, NicoleA Kratochwil, JayP Slack, Wolfgang Meyerhof

Index: BMC Struct. Biol. 7 , 66, (2007)

Full Text: HTML

Abstract

Differences in sweet taste perception among species depend on structural variations of the sweet taste receptor. The commercially used isovanillyl sweetener neohesperidin dihydrochalcone activates the human but not the rat sweet receptor TAS1R2+TAS1R3. Analysis of interspecies combinations and chimeras of rat and human TAS1R2+TAS1R3 suggested that the heptahelical domain of human TAS1R3 is crucial for the activation of the sweet receptor by neohesperidin dihydrochalcone.


Related Compounds

Related Articles:

Protective effects of neohesperidin dihydrochalcone against carbon tetrachloride-induced oxidative damage in vivo and in vitro.

2014-04-01

[Chem. Biol. Interact. 213 , 51-9, (2014)]

Determination of high-intensity sweeteners in river water and wastewater by solid-phase extraction and liquid chromatography-tandem mass spectrometry.

2015-05-08

[J. Chromatogr. A. 1393 , 106-14, (2015)]

Neohesperidin dihydrochalcone: presentation of a small molecule activator of mammalian alpha-amylase as an allosteric effector.

2013-03-18

[FEBS Lett. 587(6) , 652-8, (2013)]

Determination of nine high-intensity sweeteners in various foods by high-performance liquid chromatography with mass spectrometric detection.

2011-06-01

[Anal. Bioanal. Chem 400 , 2159-72, (2011)]

Metabolic engineering of plant cells for biotransformation of hesperedin into neohesperidin, a substrate for production of the low-calorie sweetener and flavor enhancer NHDC.

2005-12-14

[J. Agric. Food Chem. 53(25) , 9708-12, (2005)]

More Articles...