Cranbury, NJ, United States

Amicus Therapeutics

www.amicusrx.com
Cranbury, NJ, United States

Time filter

Source Type

Patent
Amicus Therapeutics | Date: 2016-10-31

Provided are in vitro and in vivo methods for determining whether a patient with Fabry disease will respond to treatment with a specific pharmacological chaperone.


Described herein are dosing regimens and kits for the treatment and/or prevention of lysosomal storage disorders such as Gaucher disease. Also described are dosing regimens and kits for the treatment and/or prevention of degenerative disorders of the central nervous system, such as the synucleinopathies Parkinsons disease or Lewy Body Dementia.


Provided is a method of increasing the stability of wild-type -glucocerebrosidase. Also provided are methods of treating and/or preventing an individual having a neurological disease in which increased expression or activity of -glucocerebrosidase in the central nervous system would be beneficial. This method comprises administering an effective amount of a pharmacologic chaperone for -glucocerebrosidase, with the proviso that the individual does not have a mutation in the gene encoding -glucocerebrosidase. Further provided are -glucocerebrosidase inhibitors which have been identified as specific pharmacologic chaperones and which have been shown to increase activity of -glucocerebrosidase in vivo in the central nervous system.


The present application provides for compositions comprising high concentrations of acid -glucosidase in combination with an active site-specific chaperone for the acid -glucosidase, and methods for treating Pompe disease in a subject in need thereof, that includes a method of administering to the subject such compositions. The present application also provides methods for increasing the in vitro and in vivo stability of an acid -glucosidase enzyme formulation.


The present invention provides novel compounds


A variant, recombinant human -glucocerebrosidase protein having a mutation at one or more of the following positions: 316, 317, 321 and 145 relative to the amino acid sequence of SEQ ID NO: 1.


Described herein are variant, recombinant -glucocerebrosidase proteins characterized as having increased stability relative to recombinant wild-type -glucocerebrosidase. Also provided herein are variant, recombinant -glucocerebrosidase proteins characterized as retaining more catalytic activity relative to recombinant wild-type -glucocerebrosidase. Further described herein are variant, recombinant -glucocerebrosidase proteins that can have amino acid variations at one or more of the following positions: 316, 317, 321 and 145. Methods of making the variant, recombinant -glucocerebrosidase proteins are also described as well as methods of treating patients having lysosomal storage diseases.


Patent
Amicus Therapeutics | Date: 2017-02-22

Described herein are dosing regimens and kits for the treatment and/or prevention of cerebral amyloidoses such as Alzheimers disease (AD) and/or cerebral amyloid angiopathy (CAA).


The present application provides compositions comprising -galactosidase A in combination with an active site-specific chaperone for the -galactosidase A, and methods for treating Fabry disease in a subject in need thereof, that includes a method of administering to the subject such compositions. The present application also provides methods for increasing the in vitro and in vivo stability of an -galactosidase A enzyme formulation. The present application also provides methods for treating Fabry disease using intravenous administration of 1-deoxygalactonojirimycin.


Patent
Amicus Therapeutics | Date: 2017-08-09

Recombinant human alpha glucosidase (rhGAA) composition derived from CHO cells that contains a more optimized glycan composition consisting of a higher amount of rhGAA containing N-glycans carrying mannose-6-phosphate (M6P) or bis-M6P than conventional rhGAAs, along with low amount of non-phosphorylated high mannose glycans, and low amount of terminal galactose on complex oligosaccharides. Compositions containing the rhGAA, and methods of use are described.

Loading Amicus Therapeutics collaborators
Loading Amicus Therapeutics collaborators