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. 2022 May 10;19:33. doi: 10.1186/s12989-022-00467-w

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© The Author(s) 2022

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 8 — CuO NPs trigger unfolding of SOD1. a SOD1 is a dimeric protein comprised of an eight-stranded β-barrel with one Cu (orange) and Zn (cyan) ion bound in each monomer. Reproduced from: Trist BG, Hilton JB, Hare DJ, Crouch PJ, Double KL. Superoxide dismutase 1 in health and disease: how a frontline antioxidant becomes neurotoxic. Angew Chem Int Ed Engl. 2021;60(17):9215–46 under a Creative Commons license (CC BY 4.0). b–e CD spectroscopy measurements were performed to assess conformational changes in recombinant human SOD1. b CuO NPs decreased the α-helix and β-sheet conformation of the SOD1 protein. c CuO NPs dissolved in ALF (pH 4.5) shifted the α-helix conformation of SOD1 protein from 208 to 212 nm. d CuCl₂ caused only a minor effect on the α-helical content, while e ZnCl₂ showed no effect. ZnO NPs could not be studied due to assay interference