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Author Grande Ribó, Núria |
Abstract Transthyretin-related diseases (TTR) are a group of rare diseases that affect the peripheral nerves and other vital organs due to the formation of amyloid deposits of this protein. Stabilization of the tetrameric structure of TTR is one of the current pharmacological strategies to prevent TTR-associated amyloidosis, such as familial amyloid polyneuropathy (FAP) and familial amyloid cardiomyopathy (FAC). The IQS Biochemistry Laboratory has been studying the fibril logenesi of TTR, has developed a screening bioassay to evaluate potential TTR inhibitors, and has analyzed several families of compounds based on non-steroidal anti-inflammatory drug analogs. On the other hand, the new synthetic methodologies developed in the IQS Pharmaceutical Chemistry Group are expanding the type of accessible structures to be used as potential inhibitors of TTR-associated amyloidosis. Specifically, this project focuses on the design and synthesis of new reversible covalent inhibitors borilats with biphenyl bisboronic acid structure that have been prepared by means of a series of new functionalization reactions catalyzed by transition metals. In the near future, the goal is to evaluate them as possible TTR inhibitors by bioassay with recombinant human TTR. The new structures could prevent unwanted off-target hormonal or anti-inflammatory activity. |
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Director Planas Sauter, Antoni |
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Degree IQS SE - Undergraduate Program in Chemistry |
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Date 2020-09-08
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