Chimeric T1R2 and T1R3 Proteins for Sweet Taste Detection
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Solution Overview
Problem
Current methods for detecting sweet taste substances or sweet taste-regulating substances using sweet taste receptors are not effective in distinguishing between activators and inhibitors, and do not offer high sensitivity.
Innovation Solution
The use of chimeric T1R2 and T1R3 proteins, specifically designed by fusing regions from human and mouse T1R2 and T1R3 proteins, and a chimeric G protein α subunit, to enhance the detection of sweet taste substances by increasing the sensitivity of the interaction with test substances, measured through changes in intracellular calcium ion concentration.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Measurement precision
If naturally occurring T1R2 and T1R3 proteins are used for detection, then the detection system is simple, but the sensitivity and ability to distinguish activators from inhibitors is insufficient
Solution Approach 1:
The patent applies composite materials by creating chimeric proteins that combine domains from different species (human and mouse T1R2/T1R3). The chimeric T1R2 consists of human T1R2 N-terminal domain (positions 1-470) fused with mouse T1R2 C-terminal domain (positions 475-843), and similarly for T1R3. This composite structure enhances detection sensitivity and specificity while maintaining functional capability.
Solution Approach 2:
The patent applies local quality by specifically modifying certain regions of the T1R2 and T1R3 proteins while preserving other regions. The chimeric construction targets specific domains (N-terminal and C-terminal regions) to optimize ligand binding and signal transduction properties, thereby improving detection precision without unnecessarily complicating the entire protein structure.
2Measurement precision
If chimeric T1R2 and T1R3 proteins with specific structures are used, then detection sensitivity is improved, but the protein structure becomes more complex
Solution Approach 1:
The patent applies segmentation by dividing the T1R2 and T1R3 proteins into distinct functional domains that can be independently optimized. The chimeric proteins are constructed by fusing specific segments from human and mouse sequences at defined boundaries (positions 470/475 for T1R2 and 63/64 for T1R3), allowing each segment to contribute its optimal properties to the overall detection function.
3Measurement precision
If conventional detection methods are used, then the detection system is easy to operate, but the ability to distinguish sweet taste activators from regulators is limited
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence parameters of the T1R2 and T1R3 proteins through chimeric construction. This changes the binding characteristics and signal transduction properties of the receptors, enabling them to distinguish between different types of sweet taste substances (activators versus regulators) with higher accuracy.
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The chimeric proteins and cells expressing them demonstrate higher sensitivity in detecting sweet taste substances, allowing for more accurate identification of activators and potentially regulating substances compared to naturally occurring T1R2 and T1R3 proteins.
Implementation Method 1
A part of taste receptors are identified as seven-transmembrane G protein-coupled receptors (GPCR) belonging to the T1R family... the heterodimer consisting of Tl R2 and T1R3 functions as a sweet taste receptor
Data Source
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AI summary
A sweet taste substance or a sweet taste-regulating substance is detected by contacting a test substance with a cell that expresses a chimeric protein of human T1R2 and mouse T1R2, and/or a chimeric protein of human T1R3 and mouse T1R3, and preferably further expresses a G protein α subunit, and by detecting an interaction of the chimeric proteins and the test substance.