Cellular and Molecular Life Sciences CMLS

, Volume 63, Issue 16, pp 1876–1888 | Cite as

Natural sweet macromolecules: how sweet proteins work

Review

Abstract.

A few proteins, discovered mainly in tropical fruits, have a distinct sweet taste. These proteins have played an important role towards a molecular understanding of the mechanisms of taste. Owing to the huge difference in size, between most sweeteners and sweet proteins, it was believed that they must interact with a different receptor from that of small molecular weight sweeteners. Recent modelling studies have shown that the single sweet taste receptor has multiple active sites and that the mechanism of interaction of sweet proteins is intrinsically different from that of small sweeteners. Small molecular weight sweeteners occupy small receptor cavities inside two subdomains of the receptor, whereas sweet proteins can interact with the sweet receptor according to a mechanism called the ‘wedge model’ in which they bind to a large external cavity. This review describes these mechanisms and outlines a history of sweet proteins.

Keywords.

Sweeteners taste receptor modelling sweet proteins food 

Copyright information

© Birkhäuser Verlag, Basel 2006

Authors and Affiliations

  1. 1.Università di Napoli Federico IINaplesItaly
  2. 2.National Institute for Medical ResearchLondonUK

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