Pipeline

AZ01 is a long acting form of interferon beta for the treatment of RRMS. Interferon beta is currently the most widely prescribed therapy for RRMS patients. AZ01 is a subcutaneously administered and long-acting form of interferon beta which is constructed using the E. coli-based CAESAR Biociphering™ platform. This platform allows for the site-specific attachment of a PEG polymer to the modified interferon beta, which results not only in an improved half-life but also a slow release pharmacological profile that has the potential to result in a less frequent dosing regimen, superior tolerability, and greater efficacy, due to increased patient compliance compared to currently prescribed interferon beta therapies.

AZ17 is a bispecific antibody capable of binding two different targets simultaneously. The site specific linkage of AZ17’s two binding domains is a product of our proprietary CAESAR Biociphering™ platform. Potential therapeutic use of AZ17 is for chronic autoimmune and inflammatory conditions, such as Crohn’s disease. AZ17 is currently in preclinical development to be followed by a Phase I clinical trial.

We have developed a platform for the introduction of non natural-amino acids into proteins expressed in the mammalian expression systems that are required for producing monoclonal antibodies. This method is proprietary to us and involves the engineering of the manufacturing cell line to deliver the non-natural amino acid at any specific position that enables efficient and effective drug conjugation. The chemical conjugation of highly potent cytotoxic drugs to monoclonal antibodies has proven to be an effective means of targeted delivery of drugs, to cancer cells, that would otherwise be too toxic for systemic administration. We have also developed special chemical conjugation chemistries that provide a highly stable hinge that is perfectly suited for use in monoclonal antibodies. The ability to conjugate a toxin that can be readily positioned at specific sites in the antibody allows full function of the antibody and effective delivery of the toxin.

Platform and Pipeline at ALLOZYNE
Scientific Publications

Wang A, Nairn NW, Johnson RS, Tirrell DA, Grabstein. Processing of N-terminal unnatural amino acids in recombinant human interferon-beta in Escherichia coli. Chembiochem. 2008, 9, 324 – 330.

Wang A. Therapeutic Protein Engineering via the Incorporation of Non-natural Amino Acids. Ehrlich II – 2nd World Conference on Magic Bullets Oct 3-5 2008, Nurnberg, Germany
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Nairn NW, Graddis TJ, Wang A, Shanebeck K, and Grabstein K. Site-specific PEGylation of interferon–beta by Cu(I)–catalyzed cycloaddition. 234th American Chemical Society National Meeting, 2007, Boston MA.
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Link J, Mock ML, Tirrell DA. Non-canonical amino acids in protein engineering. Current Opinion in Biotechnology. 2003, 14: 603-609.

Kiick KL, Saxon E, Tirrell DA, Bertozzi CR. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proceedings of the National Academy of Sciences. 2002, 99: 19-24.

Kiick KL, Tirrell DA. Protein engineering by in vivo incorporation of non-natural amino acids: control of incorporation of methionine analogues by methionyl-tRNA synthetase. Tetrahedron. 2000, 56: 9487-9493.

If you are interested in receiving information on these publications please email bd@allozyne.com