ArticleChembiochem : a European journal of chemical biology2014
Design, synthesis and characterization of fMLF-mimicking AApeptides.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
7 citing papers in PubMed, 10 citations in OpenAlex.
- Studying Neutrophil Function in vitro: Cell Models and Environmental Factors.Journal of inflammation research · 2021Review
- Chemotactic Ligands that Activate G-Protein-Coupled Formylpeptide Receptors.International journal of molecular sciences · 2019Review
- γ-AApeptides as a New Strategy for Therapeutic Development.Current medicinal chemistry · 2019Review
- Advances in Development of Antimicrobial Peptidomimetics as Potential Drugs.Molecules (Basel, Switzerland) · 2017Review
- The Formyl Peptide Receptors: Diversity of Ligands and Mechanism for Recognition.Molecules (Basel, Switzerland) · 2017Review
- γ-AApeptides as a New Class of Peptidomimetics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2016Article
- γ-AApeptides: Design, Structure, and Applications.Accounts of chemical research · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The tripeptide N-formyl-Met-Leu-Phe (fMLF) is a potent neutrophil chemoattractant and the reference agonist for the G protein-coupled N-formylpeptide receptor (FPR). As it plays a very important role in host defense and inflammation, there has been considerable interest in the development of fMLF analogues in the hope of identifying potential therapeutic agents. Herein we report the design, synthesis, and evaluation of AApeptides that mimic the structure and function of fMLF. The lead AApeptides induced calcium mobilization and mitogen-activated protein kinase (MAPK) signal transduction pathways in FPR-transfected rat basophilic leukemic (RBL) cells. More intriguingly, at high concentrations, certain AApeptides were more effective than fMLF in the induction of calcium mobilization. Their agonistic activity is further supported by their ability to stimulate chemotaxis and the production of superoxide in HL-60 cells. Similarly to fMLF, these AApeptides are much more selective towards FPR1 than FPR2. These results suggest that the fMLF-mimicking AApeptides might emerge as a new class of therapeutic agents that target FPRs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.