ArticleProtein science : a publication of the Protein Society2000
Conformational transitions and fibrillation mechanism of human calcitonin as studied by high-resolution solid-state 13C NMR.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 122 citations in OpenAlex.
- Article
- Computational insights into the aggregation mechanism of human calcitonin.International journal of biological macromolecules · 2025Article
- Molecular Insights into the Effects of F16L and F19L Substitutions on the Conformation and Aggregation Dynamics of Human Calcitonin.Journal of chemical information and modeling · 2024Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Unraveling the underlying mechanisms of reduced amyloidogenic properties in human calcitonin via double mutations.Protein science : a publication of the Protein Society · 2024Article
- Deciphering the influence of Y12L and N17H substitutions on the conformation and oligomerization of human calcitonin.Soft matter · 2024Article
- Investigating the inhibitory property of DM hCT on hCT fibrillization via its relevant peptide fragments.Protein science : a publication of the Protein Society · 2023Article
- Structural Perturbation of Monomers Determines the Amyloid Aggregation Propensity of Calcitonin Variants.Journal of chemical information and modeling · 2023Article
- Bolaamphiphilic Bis-Dehydropeptide Hydrogels as Potential Drug Release Systems.Gels (Basel, Switzerland) · 2021Article
- Fibrillation of Human Calcitonin and Its Analogs: Effects of Phosphorylation and Disulfide Reduction.Biophysical journal · 2021Article
- Impact of Citrate and Lipid-Functionalized Magnetic Nanoparticles in Dehydropeptide Supramolecular Magnetogels: Properties, Design and Drug Release.Nanomaterials (Basel, Switzerland) · 2020Article
- Flavonoids with Vicinal Hydroxyl Groups Inhibit Human Calcitonin Amyloid Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Effects of disulfide bond and cholesterol derivatives on human calcitonin amyloid formation.Biopolymers · 2020Article
- Recent progress on understanding the mechanisms of amyloid nucleation.Biophysical reviews · 2018Review
- Oil Palm Phenolics Inhibit theInternational journal of Alzheimer's disease · 2018Article
- Growth-incompetent monomers of human calcitonin lead to a noncanonical direct relationship between peptide concentration and aggregation lag time.The Journal of biological chemistry · 2017Article
- The Impact of Mathematical Modeling in Understanding the Mechanisms Underlying Neurodegeneration: Evolving Dimensions and Future Directions.CPT: pharmacometrics & systems pharmacology · 2017Review
- How Glycosaminoglycans Promote Fibrillation of Salmon Calcitonin.The Journal of biological chemistry · 2016Article
- Experimental Model System to Study pH Shift-Induced Aggregation of Monoclonal Antibodies Under Controlled Conditions.Pharmaceutical research · 2016Article
- Nucleus factory on cavitation bubble for amyloid β fibril.Scientific reports · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational transitions of human calcitonin (hCT) during fibril formation in the acidic and neutral conditions were investigated by high-resolution solid-state 13C NMR spectroscopy. In aqueous acetic acid solution (pH 3.3), a local alpha-helical form is present around Gly10 whereas a random coil form is dominant as viewed from Phe22, Ala26, and Ala31 in the monomer form on the basis of the 13C chemical shifts. On the other hand, a local beta-sheet form as viewed from Gly10 and Phe22, and both beta-sheet and random coil as viewed from Ala26 and Ala31 were detected in the fibril at pH 3.3. The results indicate that conformational transitions from alpha-helix to beta-sheet, and from random coil to beta-sheet forms occurred in the central and C-terminus regions, respectively, during the fibril formation. The increased 13C resonance intensities of fibrils after a certain delay time suggests that the fibrillation can be explained by a two-step reaction mechanism in which the first step is a homogeneous association to form a nucleus, and the second step is an autocatalytic heterogeneous fibrillation. In contrast to the fibril at pH 3.3, the fibril at pH 7.5 formed a local beta-sheet conformation at the central region and exhibited a random coil at the C-terminus region. Not only a hydrophobic interaction among the amphiphilic alpha-helices, but also an electrostatic interaction between charged side chains can play an important role for the fibril formation at pH 7.5 and 3.3 acting as electrostatically favorable and unfavorable interactions, respectively. These results suggest that hCT fibrils are formed by stacking antiparallel beta-sheets at pH 7.5 and a mixture of antiparallel and parallel beta-sheets at pH 3.3.
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