AI Article Synopsis
- Protein misfolding diseases occur when proteins struggle to achieve or maintain their correct three-dimensional shape, leading to health issues.
- In 2011, tafamidis became the first small molecule approved to treat a protein misfolding disease by specifically binding to the folded state of proteins.
- Since then, three more similar drugs have been approved, which stabilize native protein states to prevent misfolding and aggregation, showcasing how this approach can effectively address various human health problems.
Article 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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| http://dx.doi.org/10.1016/j.sbi.2021.11.009 | DOI Listing |
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