α-Sila-Dipeptides: Synthesis and Characterization.

The first two α-sila-dipeptides, 7 and cyclo-sila-dipeptide 8, were synthesized and characterized by several methods, including X-ray crystallography. Bulky t-BuMe Si substituents provide some kinetic stabilization to the synthesized molecules. 7 and 8 are the first examples of a "Si for C switch" in the central α-position of an amino acid or a peptide, in which silicon is bonded to both the amino and the carbonyl groups.

Preclinical and first-in-human evaluation of PRX-105, a PEGylated, plant-derived, recombinant human acetylcholinesterase-R.

PRX-105 is a plant-derived recombinant version of the human 'read-through' acetylcholinesterase splice variant (AChE-R). Its active site structure is similar to that of the synaptic variant, and it displays the same affinity towards organophosphorus (OP) compounds. As such, PRX-105 may serve as a bio-scavenger for OP pesticides and chemical warfare agents.

Characterization of a chemically modified plant cell culture expressed human α-Galactosidase-A enzyme for treatment of Fabry disease.

Fabry disease is an X-linked recessive disorder caused by the loss of function of the lysosomal enzyme α-Galactosidase-A. Although two enzyme replacement therapies (ERTs) are commercially available, they may not effectively reverse some of the Fabry pathology. PRX-102 is a novel enzyme for the therapy of Fabry disease expressed in a BY2 Tobacco cell culture.