Insights from microcanonical thermostatistics into amylin analogues and amyloid- $${\upbeta }$$ β cross-seeding

Rafael B. Frigori ()
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Rafael B. Frigori: Universidade Tecnológica Federal do Paraná

The European Physical Journal B: Condensed Matter and Complex Systems, 2024, vol. 97, issue 10, 1-6

Abstract: Abstract Growing evidence from population studies and clinical observations strongly suggests a complex connection between major proteinopathies, to know, Type 2 diabetes (T2D) and Alzheimer’s disease (AD). People with T2D face a significantly higher risk of developing AD compared to those without diabetes. These two conditions share several key features, such as inflammation, oxidative stress, metabolic dysfunction, and the buildup of certain proteins known as beta-amyloid (A $$\upbeta $$ β 42) and pancreatic islet amyloid polypeptide (IAPP or amylin). In AD, the brain develops characteristic senile plaques mainly composed of A $$\upbeta $$ β 42. Similarly, in individuals with T2D, the pancreas shows deposits of a protein called human amylin (hIAPP). The accumulation of these aggregated proteins in both the brain and pancreas has been associated with impaired cell function and even cell death. To gain molecular insight in the outset of such complex scenario, we perform microcanonical thermostatistics analysis of Monte Carlo simulations of A $$\upbeta $$ β 42 cross-seeded by hIAPP, or its biotechnological therapeutic analogous as Pramlintide. We find that while A $$\upbeta $$ β 42 is quite prone to cross-seed with hIAPP, and then to aggregate around that critical nuclei, this can be abolished for some of its analogues, which may possibly lead to alternative therapeutic approaches to T2D and AD. Graphic abstract

Date: 2024
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DOI: 10.1140/epjb/s10051-024-00796-z

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