Influence of selective fluorination on the biological activity and proteolytic stability of glucagon-like peptide-1
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Updated: Jun 28, 2026

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation
Published on: January 9, 2019
He Meng1, Subrahmanian Tarakkad Krishnaji, Martin Beinborn
1Department of Chemistry, Tufts University, Medford, Massachusetts 02155, USA.
Abstract:
The relative simplicity and high specificity of peptide therapeutics has fueled recent interest. However, peptide and protein drugs generally require injection and suffer from low metabolic stability. We report here the design, synthesis, and characterization of fluorinated analogues of the gut hormone peptide, GLP-1. Overall, fluorinated GLP-1 analogues displayed higher proteolytic stability with simultaneous retention of biological activity (efficacy). Fluorinated amino acids are useful for engineering peptide drug candidates and probing ligand-receptor interactions.
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