Publication | Open Access
Design and Evaluation of New Analogs of the Sweet Protein Brazzein
25
Citations
14
References
2009
Year
Brazzein-receptor Interaction ModelBioorganic ChemistryEngineeringMolecular BiologySweet Protein BrazzeinProtein RefoldingSweet Taste ReceptorEnzymatic ModificationNew AnalogsFood ChemistryProtein ChemistryBiochemistryReceptor (Biochemistry)Alternative Protein SourceBiomolecular InteractionBiomolecular EngineeringFunctional SelectivityNatural SciencesBiotechnologyProtein EngineeringMolecular Docking
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.
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