Pharmacological Chaperones

	What’s Missing in Lysosomal Storage Diseases? (pdf - 6.5MB)     About Pharmacological Chaperones (pdf - 3.4MB)

At Amicus, we have developed a novel approach to address human genetic diseases resulting from misfolded proteins. We use small molecule drugs, which are called pharmacological chaperones, to selectively bind to a target protein and increase its stability. The binding of the chaperone molecule helps the protein fold into its correct three-dimensional shape. This allows the protein to be trafficked from the ER to the appropriate location in the cell, thereby increasing protein activity and cellular function and reducing stress on cells.

We believe that our pharmacological chaperone compounds will:

Restore Protein Function
Because of the interaction with the pharmacological chaperones, the target proteins are able to pass through the quality control system of the ER and be trafficked to their appropriate location within the cell where they are biologically active. In this way, proteins are delivered where it matters.

Eliminate Aggregation and/or Accumulation of Misfolded Protein
Restoring trafficking of misfolded proteins by reducing their retention in the ER has the added potential benefit of alleviating the proteotoxic effects associated with mutant protein accumulation and/or aggregation. Thus, our pharmacological chaperones restore protein function and trafficking how it matters.

Pharmacological chaperones offer potential advantages over competing approaches to treating genetic disorders, including oral delivery and the ability to increase enzyme activity levels in tissues that are hard to reach, such as the central nervous system.