Natural sweet macromolecules: how sweet proteins work |
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Authors: | P A Temussi |
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Institution: | (1) Università di Napoli Federico II, via Cinthia 45, Naples, 80126, Italy;(2) National Institute for Medical Research, The Ridgeway, London, NW7 1AA, UK |
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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.
Received 11 February 2006; received after revision 31 March 2006; accepted 11 May 2006 |
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Keywords: | Sweeteners taste receptor modelling sweet proteins food |
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