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Updated: Oct 7, 2025

4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Small molecule protein binding to correct cellular folding or stabilize the native state against misfolding and
Fabrizio Chiti1, Jeffery W Kelly2
1Section of Biochemistry, Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Florence, Viale GB Morgagni 50, 50134 Florence, Italy.
Abstract:
Protein misfolding diseases are caused by the difficulty of a protein to attain or stably maintain its native three-dimensional structure. In 2011, the first small molecule that specifically binds to the folded state of a protein was approved by a regulatory agency to treat a protein misfolding disease (tafamidis, transthyretin amyloidosis). Subsequently, folded state binders for three additional pathologies were approved. All of these molecules bind specifically to and stabilize the native state of a misfolding-prone protein and either correct cellular folding or stabilize the native state against misfolding and aggregation. We will use these four case studies to explain how protein folding coupled to small molecule binding is a promising approach to treat a variety of human maladies.
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