I am a PhD student in Anders Olofsson lab. my research focuses on the molecular mechanisms underlying protein misfolding diseases, particularly transthyretin (TTR) amyloidosis.
I am a doctoral student in Anders Olofsson lab at the Department of Clinical Microbiology at Umeå University). Under the supervision of Professor Anders Olofsson, my research focuses on the molecular mechanisms underlying protein misfolding diseases, particularly transthyretin (TTR) amyloidosis.
In my recent study published in The Journal of Biological Chemistry, I investigated how the redox environment and macromolecular crowding influence TTR misfolding in vivo. I discovered that the formation of nonnative pathological TTR species, enriched in the plasma of TTR-Val30Met gene carriers, is promoted under oxidative conditions and suppressed by reducing agents. Additionally, I found that macromolecular crowding, such as that in plasma, can inhibit this misfolding, suggesting that the local protein concentration and environmental factors play crucial roles in TTR stability.
In addition to academic research, I am a co-inventor of a Swedish patent (SE2350342A1) that proposes a novel redox-based strategy to prevent or reverse TTR aggregation using thiol- and disulfide-modifying agents such as N-acetylcysteine.
Through interdisciplinary work, I aim to contribute to a deeper understanding of molecular disease mechanisms and support the development of novel, cost-effective therapeutic approaches.