
Exploring the structural properties and therapeutic potential of the Hsp70 chaperone’s substrate-binding domain for the treatment of amyloidosis
Project code: 09I03-03-V04-00116
Amyloidosis is a group of diseases characterized by the improper folding and aggregation of light chain, leading to their deposition in various tissues. This impairs their functionality and results in serious health complications. Despite the severity of amyloidosis, there is currently no effective treatment aimed at suppressing light chain aggregation. In this project, we plan to elucidate the structural properties and therapeutic potential of the substrate-binding domain of the chaperone Hsp70 as a novel strategy to combat amyloidosis. To achieve this, we will employ a combination of molecular biology, biophysics, and structural biology techniques. The added value of the project lies in the establishment of protein crystallography as a new scientific discipline at UPJS, both at practical and theoretical levels.
Principal Investigator: RNDr. Michal Nemergut, PhD.
Period: 07/2024 – 06/2026