ArticleMetabolic syndrome and related disorders2013
Synthesis and characterization of a novel inhibitor of C-reactive protein-mediated proinflammatory effects.
Article in Metabolic syndrome and related disorders, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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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Who cites it
3 citing papers in PubMed, 10 citations in OpenAlex.
- A novel phosphocholine-mimetic inhibits a pro-inflammatory conformational change in C-reactive protein.EMBO molecular medicine · 2023Article
- Unraveling the Antioxidant, Binding and Health-Protecting Properties of Phenolic Compounds of Beers with Main Human Serum Proteins: In Vitro and In Silico Approaches.Molecules (Basel, Switzerland) · 2020Article
- A novel peptide inhibitor attenuates C-reactive protein's pro-inflammatory effects in-vivo.International journal of cardiology · 2013Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
backgroundNumerous studies have shown that high C-reactive protein (CRP) levels predict cardiovascular disease and augur a poor prognosis in patients with acute coronary syndromes. Much in vitro and in vivo data support of a role for CRP in atherogenesis. There is an urgent need to develop inhibitors that specifically block the biological effects of CRP in vivo. The one-bead-one-compound (OBOC) combinatorial library method has been used to discover ligands against several biological targets. In this study, we use a novel fluorescence-based screening method to screen an OBOC combinatorial library for the discovery of peptides against human CRP.
methodsHuman CRP was labeled with fluorescein isothiocyanate (FITC) and human serum albumin (HuSA) was labeled with phycoerythrin (PE) and used for screening. The OBOC library LWH-01 was synthesized on TentaGel resin beads using a standard solid-phase "split/mix" approach.
resultsBy subtraction screening, eight peptides that bind specifically to CRP and not to HuSA were identified. In human aortic endothelial cells (HAECs) incubated with CRP, inhibitors CRPi-2, CRPi-3, and CRPi-6 significantly inhibited CRP-induced superoxide, cytokine release, and nuclear factor-κB (NFκB) activity. Molecular docking studies demonstrate that CRPi-2 interacts with the two Ca(2+) ions in the single subunit of CRP. The binding of CRPi-2 is reminiscent of choline binding.
conclusionsFuture studies will examine the utility of this inhibitor in animal models and clinical trials.
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