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Chemical Senses Advance Access originally published online on August 20, 2009
Chemical Senses 2009 34(8):679-683; doi:10.1093/chemse/bjp048
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Design and Evaluation of New Analogs of the Sweet Protein Brazzein

D. Eric Walters1, Tiffany Cragin2, Zheyuan Jin2, Jon N. Rumbley3 and Göran Hellekant2

1 Department of Biochemistry and Molecular Biology, The Chicago Medical School, Rosalind Franklin University of Medicine and Science, 3333 Green Bay Road, North Chicago, IL 60064, USA 2 Department of Physiology and Pharmacology, Medical School, University of Minnesota Duluth, 1035 University Drive, Duluth, MN 55812, USA 3 Department of Pharmacy Practice and Pharmaceutical Sciences, College of Pharmacy, University of Minnesota Duluth, 1110 Kirby Drive, Duluth, MN 55812, USA

Correspondence to be sent to: D. Eric Walters, Department of Biochemistry and Molecular Biology, The Chicago Medical School, Rosalind Franklin University of Medicine and Science, 3333 Green Bay Road, North Chicago, Illinois 60064 USA. email: eric.walters{at}rosalindfranklin.edu, telephone: 847-578-8613, fax: 847-542-4740


  Abstract

We have previously modeled the interaction of the sweet protein brazzein with the extracellular domains of the sweet taste receptor. Here, we describe the application of that model to the design of 12 new highly potent analogs of brazzein. Eight of the 12 analogs have higher sweetness potency than wild-type brazzein. Results are consistent with our brazzein–receptor interaction model. The model predicts binding of brazzein to the open form of T1R2 in the T1R2–T1R3 heterodimer.

Key words: brazzein, labeled magnitude scale, Pentadiplandra brazzeana, psychophysics, sweetener, taste receptor

Accepted 27 July 2009


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