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May 7, 2026ACS Medicinal Chemistry Letters0 citationsOpen Access

Characterizing Agonist And Antagonist Peptide Binding Kinetics To GLP-1R Using Surface Plasmon...

In Vitro Characterization of Agonist and Antagonist Peptide Binding Interaction Kinetics to GLP-1R in HEK293T Cells Using Surface Plasmon Resonance Microscopy

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Authors

MTMiyuki A. ThirumurthyJLJesús S. Aguilar Díaz de leónSPShuchong Pan

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Overview

Randomized trial demonstrates binding kinetics of GLP-1R interactions with peptides, indicating implications for drug design.

Key Points

  • This research aims to characterize the binding interaction kinetics of agonists and antagonists to the GLP-1 receptor (GLP-1R).
  • Employed surface plasmon resonance microscopy (SPRM) on HEK293T cells overexpressing GLP-1R
  • Visualized and quantified label-free kinetic interactions of ligands in real time
  • Analyzed binding behaviors of three agonists (GLP-1, liraglutide, exendin-4) and one antagonist (exendin-9).
  • Agonists showed two-mode binding with C-terminal engagement of the extracellular domain and N-terminal engagement of the transmembrane domain.
  • The antagonist exendin-9 demonstrated single-mode binding only to the extracellular domain.
  • Liraglutide exhibited the highest binding affinity and activation through transmembrane domain engagement.

Cite This Study

Thirumurthy et al. (2026) studied this question.

synapsesocial.com/papers/69fc2b608b49bacb8b3477dbhttps://doi.org/10.1021/acsmedchemlett.6c00091
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