ArticleScientific reports2017
Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 70 citations in OpenAlex.
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- Enhanced Bioavailability of Dihydrotanshinone I-Bovine Serum Albumin Nanoparticles for Stroke Therapy.Frontiers in pharmacology · 2021Article
- Effects of Eugenol on Memory Performance, Neurogenesis, and Dendritic Complexity of Neurons in Mice Analyzed by Behavioral Tests and Golgi Staining of Brain Tissue.Journal of stem cells & regenerative medicine · 2021Article
- Molecular Interaction of Protein-Pigment C-Phycocyanin with Bovine Serum Albumin in a Gomphosis Structure Inhibiting Amyloid Formation.International journal of molecular sciences · 2020Article
- Article
- Lead optimization for promising monoamine oxidase inhibitor from eugenol for the treatment of neurological disorder: synthesis and in silico based study.BMC chemistry · 2019Article
- Amino Acid Based Self-assembled Nanostructures: Complex Structures from Remarkably Simple Building Blocks.ChemNanoMat : chemistry of nanomaterials for energy, biology and more · 2018Article
- Intrinsic property of phenylalanine to trigger protein aggregation and hemolysis has a direct relevance to phenylketonuria.Scientific reports · 2017Article
- Effects of a combination treatment of KD5040 andBMC complementary and alternative medicine · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eugenol has attracted considerable attention because of its potential for many pharmaceutical applications including anti-inflammatory, anti-tumorigenic and anti-oxidant properties. Here, we have investigated the effect of eugenol on amyloid formation of selected globular proteins. We find that both spontaneous and seed-induced aggregation processes of insulin and serum albumin (BSA) are significantly suppressed in the presence of eugenol. Isothermal titration calorimetric data predict a single binding site for eugenol-insulin complex confirming the affinity of eugenol for native soluble insulin species. We also find that eugenol suppresses amyloid-induced hemolysis. Our findings reveal the inherent ability of eugenol to stabilize native proteins and to delay the conversion of protein species of native conformation into β-sheet assembled mature fibrils, which seems to be crucial for its inhibitory effect.
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