OVERVIEW

Model of VP1-001 in its binding site in the alpha-crystallin dimer, based on PDB ID 2WJ7, as described in Science 06 Nov 2015: Vol. 350, Issue 6261, pp. 674-677

Model of VP1-001 in its binding site in the alpha-crystallin dimer, based on PDB ID 2WJ7, as described in Science 06 Nov 2015: Vol. 350, Issue 6261, pp. 674-677

We are passionately committed to the discovery, development, and commercialization of treatments for protein misfolding diseases. Protein misfolding, the change of a protein from its functional shape to a dysfunctional shape due to accumulated stress factors or modification, is implicated in numerous common disorders including cataracts, presbyopia, and neurodegenerative diseases.

Our initial focus is crystallin biology. To address the global need for new methods to treat cataracts and presbyopia, we are pioneering the development of crystallin stabilizers such as VP1-001, a molecule designed to stabilize the functional form of the crucial human lens protein alpha-crystallin against accumulated damage. By developing VP1-001 as a small molecule medicine suitable for topical application, we hope to revitalize the treatment paradigm for vision loss associated with presbyopia and cataracts.