The temperature dependence of amyloid <i>β</i> solubility reveals the hydrophobic effect as the main driving force for fibril formation
C. The remaining monomer concentration was measured after 48 to 168 h, with little change in between suggesting that equilibrium is approached at 168 h. The lowest solubility of 20 ± 10 nM is found around body temperature, with higher solubility at both lower and higher temperatures. This nonmonotonic temperature dependence is indicative of the hydrophobic effect being a major driving force for the fibril formation of this peptide.
Authors
- Max Lindberg (ORCID: https://orcid.org/0009-0008-1579-4970)
- Jing Hu (ORCID: https://orcid.org/0009-0000-3605-2185)
- Sara Snogerup Linse (ORCID: https://orcid.org/0000-0001-9629-7109)
- Emma Sparr (ORCID: https://orcid.org/0000-0001-8343-9657)
- Dev Thacker (ORCID: https://orcid.org/0000-0001-6171-9703)
Institutions
- Lund University (SE)
- Institution of Structural Engineers (GB)
- Institute of Physical Chemistry (PL)
- Institute of Structural and Molecular Biology (GB)
Publication Details
- Journal
- Proceedings of the National Academy of Sciences
- Published
- 2026-04-20
- DOI
- https://doi.org/10.1073/pnas.2531916123
- Primary Topic
- Alzheimer's disease research and treatments
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Knut och Alice Wallenbergs Stiftelse
- Vetenskapsrådet
- European Research Council