Design and evaluation of new analogs of the sweet protein brazzein

Chem Senses. 2009 Oct;34(8):679-83. doi: 10.1093/chemse/bjp048. Epub 2009 Aug 20.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adult
  • Aged
  • Escherichia coli / genetics
  • Female
  • Humans
  • Magnoliopsida / chemistry
  • Male
  • Middle Aged
  • Mutation
  • Plant Proteins / chemistry
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism*
  • Protein Binding
  • Receptors, G-Protein-Coupled / metabolism
  • Sweetening Agents / chemistry
  • Sweetening Agents / metabolism*
  • Taste Buds / metabolism
  • Taste Perception*
  • Young Adult

Substances

  • Plant Proteins
  • Receptors, G-Protein-Coupled
  • Sweetening Agents
  • brazzein protein, Pentadiplandra brazzeana
  • taste receptors, type 1