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J Med Chem. 2008 Nov 27;51(22):7303-7. doi: 10.1021/jm8008579.

Influence of selective fluorination on the biological activity and proteolytic stability of glucagon-like peptide-1.

Author information

1
Department 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.

PMID:
18950150
PMCID:
PMC2645917
DOI:
10.1021/jm8008579
[Indexed for MEDLINE]
Free PMC Article

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