ArticleNature chemistry2022
Conformational and functional changes of the native neuropeptide somatostatin occur in the presence of copper and amyloid-β.
Article in Nature chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Zinc Fingers as Programmable Metalloprotein Scaffolds for Altering Pathogenic Biomolecular Phase Transitions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Strategic physicochemical tuning: amphiphilic polymers as molecular regulators of amyloid aggregation and cytotoxicity.Chemical science · 2026Article
- Targeting de novo pyrimidine synthesis confers vulnerability to copper-mediated ATR inactivation in PARP inhibitor-resistant ovarian cancer.Nature communications · 2026Article
- Multi-omic derived cell-type specific Alzheimer disease polygenic risk scores.Neurobiology of aging · 2025Article
- Marine Natural Product Chagosendine C Induces Cuproptosis in Colorectal Cancer Cells by Targeting FDX1.Journal of the American Chemical Society · 2025Article
- Deciphering the Tumor Uptake of Heterobivalent (SSTJournal of medicinal chemistry · 2025Article
- Identification and Exploration of Immunity-Related Genes and Natural Products for Alzheimer's Disease Based on Bioinformatics, Molecular Docking, and Molecular Dynamics.Immunity, inflammation and disease · 2025Article
- From coordination to function: Inorganic insights into metalloproteins and metallopeptides in biosystems.Biophysics and physicobiology · 2025Article
- Transition metal ions and neurotransmitters: coordination chemistry and implications for neurodegeneration.RSC chemical biology · 2023Review
- Copper(II) Affects the Biochemical Behavior of Proinsulin C-peptide by Forming Ternary Complexes with Serum Albumin.Journal of the American Chemical Society · 2023Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The progression of neurodegenerative disorders can lead to impaired neurotransmission; however, the role of pathogenic factors associated with these diseases and their impact on the structures and functions of neurotransmitters have not been clearly established. Here we report the discovery that conformational and functional changes of a native neuropeptide, somatostatin (SST), occur in the presence of copper ions, metal-free amyloid-β (Aβ) and metal-bound Aβ (metal-Aβ) found as pathological factors in the brains of patients with Alzheimer's disease. These pathological elements induce the self-assembly of SST and, consequently, prevent it from binding to the receptor. In the reverse direction, SST notably modifies the aggregation profiles of Aβ species in the presence of metal ions, attenuating their cytotoxicity and interactions with cell membranes. Our work demonstrates a loss of normal function of SST as a neurotransmitter and a gain of its modulative function against metal-Aβ under pathological conditions.
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