Preprint Article Version 1 This version is not peer-reviewed

Multimodal Ligand Binding Studies of Human and Mouse G-Coupled Taste Receptors to Correlate with their Species-Specific Sweetness Properties

Version 1 : Received: 16 August 2018 / Approved: 17 August 2018 / Online: 17 August 2018 (11:15:39 CEST)

A peer-reviewed article of this Preprint also exists.

Assadi-Porter, F.M.; Radek, J.; Rao, H.; Tonelli, M. Multimodal Ligand Binding Studies of Human and Mouse G-Coupled Taste Receptors to Correlate Their Species-Specific Sweetness Tasting Properties. Molecules 2018, 23, 2531. Assadi-Porter, F.M.; Radek, J.; Rao, H.; Tonelli, M. Multimodal Ligand Binding Studies of Human and Mouse G-Coupled Taste Receptors to Correlate Their Species-Specific Sweetness Tasting Properties. Molecules 2018, 23, 2531.

Journal reference: Molecules 2018, 23, 2531
DOI: 10.3390/molecules23102531

Abstract

Taste signaling is a complex process that is linked to obesity and its associated metabolic syndromes. The sweet taste is mediated through a heterodimeric G protein coupled receptor (GPRC) in a species-specific manner and at multi-tissue specific levels. The sweet receptor recognizes a large number of ligands with structural and functional diversities to modulate different amplitudes of downstream signaling pathway(s). The human sweet-taste receptor has been extremely difficult to study by biophysical methods due to inadequate methods for producing large homogeneous quantities of the taste-receptor protein and a lack of reliable in vitro assays to precisely measure productive ligand binding modes leading to activity upon their interactions with the receptor protein. We report a multimodal high throughput assays to monitor ligand binding, receptor stability and conformational changes to model the molecular interactions between ligand-receptor. We applied saturation transfer difference nuclear magnetic resonance spectroscopy (STD-NMR) complemented by differential scanning calorimetry (DSC), circular dichroism (CD) spectroscopy, and intrinsic fluorescence spectroscopy (IF) to characterize binding interactions. Our method using complementary NMR and biophysical analysis is advantageous to study the mechanism of ligand binding and signaling processes in other GPCRs.

Subject Areas

Heterodimeric G protein coupled receptor; saturation transfer difference nuclear magnetic resonance spectroscopy; differential scanning calorimetry; circular dichroism; intrinsic fluorescence spectroscopy

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