Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a ?-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a ?-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The invention provides methods for efficient recombinant expression, refolding, and purification of Beta-site APP cleaving enzyme (BACE) polypeptides. In various aspects, the method includes the steps of expressing a recombinant construct in bacteria, dissolving inclusion bodies with a denaturant at high pH in the presence of a reducing agent, diluting the solubilized BACE polypeptide in an aqueous solution at a temperature of about 1° C. to 15° C., and incubating the diluted sample at a temperature of about 4° C. to 15° C. until the recombinant BACE polypeptide folds into an active enzyme.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a ?-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The x-ray crystal structure of human BACE or BACE-like proteins is useful for solving the structure of other molecules or molecular complexes, and identifying and/or designing potential modifiers of human BACE activity.

Abstract: The x-ray crystal structure of human BACE or BACE-like proteins is useful for solving the structure of other molecules or molecular complexes, and identifying and/or designing potential modifiers of human BACE activity.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a ?-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a &bgr;-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a &bgr;-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a &bgr;-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a &bgr;-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.

Abstract: The present invention relates to Glutathione S-transferase (GST)/Reduced Glutathione (GSH) as a means for the in-vivo release of a drug that has been conjugated to specific electrophilic moieties via a sulfonamide bond. The drug may be an anticancer agent (or one with other therapeutic properties) carrying a free —NH— which has been derivatized by the attachment of an electrophile containing a moiety, such as p-CN— or p-NO2-pyridinylsulfonyl groups, or p-NO2- or 2,4 dinitrophenylsulfonyl groups, or suitable derivatives thereof, to make a prodrug. Optionally, the sulfonamide moiety may have attached to it a targeting molecule. The present invention also provides Glutathione S-transferase (GST)/Reduced Glutathione (GSH) as a means for the release of a protected amino derivative that has been conjugated to specific electrophilic moieties via a sulfonamide bond.

Abstract: The present invention relates to Glutathione S-transferase (GST)/Reduced Glutathione (GSH) as a means for the in-vivo release of a drug that has been conjugated to specific electrophilic moieties via a sulfonamide bond. The drug may be an anticancer agent (or one with other therapeutic properties) carrying a free —NH— which has been derivatized by the attachment of an electrophile containing a moiety, such as p-CN— or p-NO 2-pyridinylsulfonyl groups, or p-NO 2- or 2,4 dinitrophenylsulfonyl groups, or suitable derivatives thereof, to make a prodrug. Optionally, the sulfonamide moiety may have attached to it a targeting molecule. The present invention also provides Glutathione S-transferase (GST)/Reduced Gluthathione (GSH) as a means for the release of a protected amino derivative that has been conjugated to specific electrophilic moieties via a sulfonamide bond.

Abstract: The present invention is directed to novel substrates for Hu-Asp. More particularly, the invention provides peptide substrates and fusion polypeptide substrates comprising a &bgr;-secretase cleavage site. Methods and compositions for making and using the peptides are disclosed.