Ion-Mediated Morphological Diversity in Protein Amyloid Systems
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Salt ions are considered among the major determinants ruling protein folding, stability, and self-assembly in the context of amyloid-related diseases, protein drug development, and functional biomaterials. Here, we report that Hofmeister ions not only determine the rate constants of the aggregation reaction for human insulin and hen egg white lysozyme but also control the generation of a plethora of amyloid-like morphologies ranging from the nanoscale to the microscale. We anticipate that the latter is a result of a balance between colloidal and conformational stability combined with an ion-specific effect and highlight the importance of salt ions in controlling the biological functions of protein aggregates.
| Original language | English |
|---|---|
| Journal | Journal of Physical Chemistry Letters |
| Volume | 13 |
| Issue number | 16 |
| Pages (from-to) | 3586-3593 |
| ISSN | 1948-7185 |
| DOIs | |
| Publication status | Published - 2022 |
Bibliographical note
Funding Information:
V.F., J.J.V., and H.C. acknowledge VILLUM FONDEN for funding the project via the Villum Young Investigator Grant “Protein Superstructures as Smart Biomaterials (ProSmart)” 2018–2023 (Grant 19175). The authors acknowledge Dr. Samuel Lenton (University of Copenhagen) for the discussion of the data. The authors acknowledge the Core Facility for Integrated Microscopy, Faculty of Health and Medical Sciences, University of Copenhagen. The authors thank the Danish Research Council for Technology and Production Sciences for funding Centrifuge 5417R. The authors thanks Carlsberg Foundation for funding the Epsilon 2-4 LSCPlus. The authors thank the VILLUM FONDEN (Grant 19175) for funding the CLARIOstar plate reader and VILLUM FONDEN (Grant 19175), the Novo Nordisk Foundation (Grant NNF16OC0021948), and Lundbeck Foundation (Grant R155-2013-14113) for funding the Leica DMi8 microscope. All schemes were created with BioRender.com.
Publisher Copyright:
© 2022 American Chemical Society.
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