ArticleBiopolymers2020
Effects of disulfide bond and cholesterol derivatives on human calcitonin amyloid formation.
Article in Biopolymers, 2020. 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, 11 citations in OpenAlex.
- Precision mRNA Delivery via Ultrasound-Controlled Release Perfluorocarbon Emulsions: An Innovative Ultrasound Theranostic Strategy withSmall (Weinheim an der Bergstrasse, Germany) · 2026Article
- Investigating the inhibitory property of DM hCT on hCT fibrillization via its relevant peptide fragments.Protein science : a publication of the Protein Society · 2023Article
- Flavonoids with Vicinal Hydroxyl Groups Inhibit Human Calcitonin Amyloid Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
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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 that aggregates to form amyloid fibrils under appropriate conditions. In this study, we investigated the effect of the intramolecular disulfide bond formed at the N-terminal region of the peptide in the aggregation kinetics of hCT. Our results indicate that the presence of the disulfide bond in hCT plays a crucial role in forming the critical nucleus needed for fibril formation, facilitating the rate of hCT amyloidogenesis. Furthermore, we reported for the first time the effects of cholesterol, cholesterol sulfate, and 3β-[N-(dimethylaminoethane)carbamoyl]-cholesterol (DC-cholesterol) on the amyloid formation of oxidized hCT. Our results show that while cholesterol does not affect amyloidogenesis of oxidized hCT, high concentrations of cholesterol sulfate exhibits a moderate inhibiting activity on hCT amyloid formation. In particular, our results show that DC-cholesterol strongly inhibits amyloidogenesis of oxidized hCT in a dose-dependent manner. Further studies at different pH conditions imply the crucial impact of electrostatic and hydrogen bonding interactions in mediating the interplay of hCT and the surface of DC-cholesterol vesicles and the inhibiting function of DC-cholesterol on hCT fibrillization.
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Registered trials
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