ArticleScientific reports2017
Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Size of Biomolecular Condensates Dictates Fate in Liquid-Solid Phase Transitions through Amorphous-Amyloid Competition.Journal of the American Chemical Society · 2026Article
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- Clinical implications of atrial natriuretic peptide amyloidosis.BMJ case reports · 2021Article
- Solid-state packing dictates the unexpected solubility of aromatic peptides.Cell reports. Physical science · 2021Article
- Epigallocatechin-3-gallate Inhibits Cu(II)-Induced β-2-Microglobulin Amyloid Formation by Binding to the Edge of Its β-Sheets.Biochemistry · 2020Article
- Amyloid and the Heart.Current cardiology reports · 2019Review
- Crystal structure of 6aJL2-R24G light chain variable domain: Does crystal packing explain amyloid fibril formation?Biochemistry and biophysics reports · 2019Article
- Zinc boosts EGCG's hIAPP amyloid Inhibition both in solution and membrane.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Computational Molecular Docking and X-ray Crystallographic Studies of Catechins in New Drug Design Strategies.Molecules (Basel, Switzerland) · 2018Review
- Novel Therapies in Light Chain Amyloidosis.Kidney international reports · 2018Review
- Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice.Scientific reports · 2018Article
- Light Chain Amyloidosis.Mediterranean journal of hematology and infectious diseases · 2018Review
- Novel pharmacotherapies for cardiac amyloidosis.Pharmacology & therapeutics · 2017Review
- Amorphous Solid Dispersion of Epigallocatechin Gallate for Enhanced Physical Stability and Controlled Release.Pharmaceuticals (Basel, Switzerland) · 2017Article
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibody light chain amyloidosis is a rare disease caused by fibril formation of secreted immunoglobulin light chains (LCs). The huge variety of antibody sequences puts a serious challenge to drug discovery. The green tea polyphenol epigallocatechin-3-gallate (EGCG) is known to interfere with fibril formation in general. Here we present solution- and solid-state NMR studies as well as MD simulations to characterise the interaction of EGCG with LC variable domains. We identified two distinct EGCG binding sites, both of which include a proline as an important recognition element. The binding sites were confirmed by site-directed mutagenesis and solid-state NMR analysis. The EGCG-induced protein complexes are unstructured. We propose a general mechanistic model for EGCG binding to a conserved site in LCs. We find that EGCG reacts selectively with amyloidogenic mutants. This makes this compound a promising lead structure, that can handle the immense sequence variability of antibody LCs.
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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.