Enzyme enhancement therapy through non-competitive pharmacological chaperones
Document typeConference report
Rights accessOpen Access
Most Pharmacological chaperones (PC’s) described until now are substrate analogues which bind to the active site of the target protein. C ons e- quently, such PC’s also inhibit the target protein at higher concentrations thus rendering a narrow therapeutic window and have poor drug-like properties. Through our proprietary technology platform SEE-Tx™, we identify a new generation of non-substrate competitive pharmacological chaperones which p o- tentially offer a much broader therapeutic window. What’s more, such co m- pounds are not substrate analogues, thus presenting much better drug-like pro p- erties, particularly for indications with CNS involvement. Here we present our methodology to identify non-competitive pharmacological chaperones applied to the enzyme beta-galactosidase, whose deficiency is related with GM1 Gangliosidosis and Morquio B.
Pharmacological chaperones, Chemical chaperones , Enzyme e n- hancement therapy, GM1, Gangliosidosis, Morqui B, Lysosomal Storage Disease, Lysosomal Storage Disorders
CitationAymami, J. [et al.]. Enzyme enhancement therapy through non-competitive pharmacological chaperones. A: IWBBIO 2014. "Proceedings IWBBIO 2014". 2014, p. 390-395.