ArticleChemistry (Weinheim an der Bergstrasse, Germany)2020
Flavonoids with Vicinal Hydroxyl Groups Inhibit Human Calcitonin Amyloid Formation.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Inhibition of amyloid formation of prion fragment (106-128) by polyphenolic compounds.Biochimica et biophysica acta. General subjects · 2025Article
- Phytochemical profiling andFrontiers in chemistry · 2024Article
- Neuroprotective Potential of Flavonoids in Brain Disorders.Brain sciences · 2023Review
- Identification of Catechins' Binding Sites in Monomeric AInternational journal of molecular sciences · 2023Article
- Structural Perturbation of Monomers Determines the Amyloid Aggregation Propensity of Calcitonin Variants.Journal of chemical information and modeling · 2023Article
- Dihydrocaffeic Acid-Decorated Iron Oxide Nanomaterials Effectively Inhibit Human Calcitonin Aggregation.ACS omega · 2022Article
- Comparative study of polyphenolic compound extraction from empty palm fruit bunches and sugarcane pulp.Heliyon · 2022Article
- Dopamine-Conjugated Carbon Dots Inhibit Human Calcitonin Fibrillation.Nanomaterials (Basel, Switzerland) · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human calcitonin (hCT) is a 32-residue peptide hormone that can aggregate into amyloid fibrils and cause cellular toxicity. In this study, we investigated the inhibition effects of a group of polyphenolic molecules on hCT amyloid formation. Our results suggest that the gallate moiety in epigallocatechin-3-gallate (EGCG), a well-recognized amyloid inhibitor, is not critical for its inhibition function in the hCT amyloid formation. Our results demonstrate that flavonoid compounds, such as myricetin, quercetin, and baicalein, that contain vicinal hydroxyl groups on the phenyl ring effectively prevent hCT fibrillization. This structural feature may also be applied to non-flavonoid polyphenolic inhibitors. Moreover, our results indicate a plausible mechanistic role of these vicinal hydroxyl groups which might include the oxidation to form a quinone and the subsequent covalent linkage with amino acid residues such as lysine or histidine in hCT. This may further disrupt the crucial electrostatic and aromatic interactions involved in the process of hCT amyloid fibril formation. The inhibition activity of the polyphenolic compounds against hCT fibril formation may likely be attributed to a combination of factors such as covalent linkage formation, aromatic stacking, and hydrogen bonding interactions.
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Registered trials
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