ArticleACS pharmacology & translational science2020
Optimization of Peptide Inhibitors of β-Klotho as Antagonists of Fibroblast Growth Factors 19 and 21.
Article in ACS pharmacology & translational science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Antagonism of β-klotho signaling by peptide 19 impairs wheel running in male mice and potentiates the cisplatin-induced decrease in wheel running.Frontiers in pharmacology · 2026Article
- Hepatic mitochondrial signaling as a systemic hub: inter-organ communication networks in aging and aging-related diseases.Frontiers in cell and developmental biology · 2026Review
- FGF21 reverses MASH through coordinated actions on the CNS and liver.Cell metabolism · 2025Article
- Branched Multimeric Peptides as Affinity Reagents for the Detection of α-Klotho Protein.Angewandte Chemie (International ed. in English) · 2023Article
- Metabolic Spectrum of Liver Failure in Type 2 Diabetes and Obesity: From NAFLD to NASH to HCC.International journal of molecular sciences · 2021Review
- Glucagon receptor signaling regulates weight loss via central KLB receptor complexes.JCI insight · 2021Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibroblast growth factors 19 and 21 (FGF19 and FGF21) have biological actions that render them promising clinical candidates for treatment of metabolic diseases, particularly dyslipidemia and nonalcoholic steatohepatitis (NASH). These two atypical endocrine FGFs employ an accessory receptor β-klotho (KLB) to signal through classical FGF receptors (FGFRs). FGF19 and FGF21 bind to KLB via their C-terminus, to orient the N-terminus for productive interaction with FGFRs. The C-terminal peptides have been shown to competitively inhibit this biological agonism. We report here an assessment of the structural relationship in the C-terminal sequences of FGF19 and FGF21 that led to the identification of a sustained-acting peptide optimized for pharmacological use. It demonstrates high potency and selectivity to antagonize FGF19 and FGF21 in cells coexpressing FGFRs and KLB. This peptide was also effective in blocking FGF19 and FGF21 mediated downstream gene expression (i.e.,
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Registered trials
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