Temperature-Dependent Aggregation of Tau Protein Is Attenuated by Native PLGA Nanoparticles Under in vitro Conditions
These results, taken together, suggest that native PLGA nanoparticles can not only attenuate temperature-dependent tau aggregation but also promote disassembly of preformed aggregates, which increased with a rise of temperature. Given the evidence that temperature can influence tau pathology, we believe that native PLGA may have a unique potential to regulate tau abnormalities associated with AD-related pathology.
Authors
- Emmanuel Planel (ORCID: https://orcid.org/0000-0001-5128-0565)
- Leonardo M. Cortez (ORCID: https://orcid.org/0000-0003-4080-8728)
- Mahalashmi Srinivasan (ORCID: https://orcid.org/0009-0006-0386-1334)
- Satyabrata Kar (ORCID: https://orcid.org/0000-0003-0167-3808)
- Valerie L. Sim (ORCID: https://orcid.org/0000-0002-0088-8666)
- Sue‐Ann Mok (ORCID: https://orcid.org/0000-0003-4593-3368)
- Holger Wille (ORCID: https://orcid.org/0000-0001-5102-8706)
- Jae‐Young Cho (ORCID: https://orcid.org/0000-0002-1868-6464)
- Aria Khalili (ORCID: https://orcid.org/0000-0001-8029-3488)
- Pallabi Sil Paul (ORCID: https://orcid.org/0000-0001-9873-9206)
- Mallesh Rathnam
Institutions
- University of Alberta (CA)
- National Institute for Nanotechnology (CA)
- Université Laval (CA)
Publication Details
- Journal
- International Journal of Nanomedicine
- Published
- 2025-02-01
- DOI
- https://doi.org/10.2147/ijn.s494104
- Citations
- 3
- Primary Topic
- Alzheimer's disease research and treatments
- Type
- article
- Field-Weighted Citation Impact
- 3.49