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GLP-1R agonists have distinct signaling profiles at the plasma membrane Based on the structural differences observed in the residue contact analysis, we selected a series of homologous peptide agonists (GLP-1 and exendin-4 analogs) in addition to the small molecule agonist (Supplementary Data 2) to investigate the pathway selectivity of GLP-1R at the plasma membrane using the effector membrane translocation assay (EMTA) based on enhanced bystander BRET (ebBRET) in living cells 5

Despite these large structural differences, the TMD pocket volume of the GLP-1RFab7F38 structure (893 3 ) is of similar scale as the ligand-occupied GLP-1R pockets (5VAI: 1036 3

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Furthermore, since the alkane chain of DDA should be the origin of the hydrophobic character of alkylamine-GSH AuNCs, we studied the hydrophobication and phase transfer of GSH-AuNCs using alkylamines with various chain length (C4, C10, C12, C16 and C18) from water to dichloromethane

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