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Xencor: Via Fc engineering enhanced antibody half-life improves in vivo activity

Improved affinity for the neonatal Fc receptor (FcRn) is known to extend antibody half-life in vivo. However, this has never been linked with enhanced therapeutic efficacy. Mr Jonathan Zalevsky and Dr John Desjarlais et al. of Xencor at Monrovia, CA, USA, studied if such enhanced antibody half-life improves in vivo activity, as published online in Nature Biotechnology on 17 January 2010.

Ustekinumab better than etanercept in psoriasis trial

In a study by Christopher Griffiths et al. of the University of Manchester, UK, Johnson & Johnson (J&J)’s monoclonal antibody STELARA (ustekinumab, an interleukin-12 and interleukin-23 blocker) and Amgen’s Enbrel (etanercept, an inhibitor of tumour necrosis factor: anti-TNF) have been compared for the treatment of psoriasis, as published in The New England Journal of Medicine (NEJM) of 14 January 2010. The Phase 3, Multicenter, Randomized Study Comparing CNTO 1275 and Etanercept for the Treatment of Moderate to Severe Plaque Psoriasis’ was sponsored by J&J’s Centocor.

FTC- Biosimilars to spur innovation and competitive prices

In the Journal of Generic Medicines (published online 8 September 2009), Michael Wroblewski and Elizabeth Jex of the US Federal Trade Commission (FTC) write about the promise of follow-on biologics (FOBs) to spur both biological drug innovation and competitive prices.

Time for a re-evaluation of ESAs

In an article in The New England Journal of Medicine (NEJM) by Ellis F Unger, Aliza M Thompson, Melanie J Blank, and Robert Temple, published on 6 January 2010 at NEJM.org, it is stated that it is time for a re-evaluation of erythropoiesis-stimulating agents (ESAs).

Modify Fc fucosylation and β-galactosylation for biobetter MAbs

In an article by Dr Claire Morgan and Dr Daryl Fernandes of Ludger, published in IPI of Autumn 2009, it is shown how both the original drug manufacturers and the designers of follow-on biologics could produce biobetter monoclonal antibodies (MAbs) through glycoengineering. (see also Ludger’s GTO-QbD: Defining glycovariant biobetter MAbs, When is a glycoengineered biobetter commercially better than a biosimilar? and Strategy and tools for building glycoengineered biobetter MAbs)

When is a glycoengineered biobetter commercially better than a biosimilar?

In an article by Dr Claire Morgan and Dr Daryl Fernandes of Ludger, published in IPI of Autumn 2009, it is shown how both the original drug manufacturers and the designers of follow-on biologics could produce biobetter monoclonal antibodies (MAbs) through glycoengineering. (see also Modify Fc fucosylation and β-galactosylation for biobetter MAbs, Design out NeuGc, Fab glycosylation for biobetter MAbs, Design out Gal-α(1,3)-Gal for biobetter MAbs, Strategy and tools for building glycoengineered biobetter MAbs and Ludger’s GTO-QbD: Defining glycovariant biobetter MAbs)

Design out NeuGc, Fab glycosylation for biobetter MAbs

In an article by Dr Claire Morgan and Dr Daryl Fernandes of Ludger, published in IPI of Autumn 2009, it is shown how both the original drug manufacturers and the designers of follow-on biologics could produce biobetter monoclonal antibodies (MAbs) through glycoengineering. (see also Ludger’s GTO-QbD: Defining glycovariant biobetter MAbs, When is a glycoengineered biobetter commercially better than a biosimilar? and Strategy and tools for building glycoengineered biobetter MAbs)

Design out Gal-α(1,3)-Gal for biobetter MAbs

In an article by Dr Claire Morgan and Dr Daryl Fernandes of Ludger, published in IPI of Autumn 2009, it is shown how both the original drug manufacturers and the designers of follow-on biologics could produce biobetter monoclonal antibodies (MAbs) through glycoengineering. (see also Ludger’s GTO-QbD: Defining glycovariant biobetter MAbs, When is a glycoengineered biobetter commercially better than a biosimilar? and Strategy and tools for building glycoengineered biobetter MAbs)

Strategy and tools for building glycoengineered biobetter MAbs

In an article by Dr Claire Morgan and Dr Daryl Fernandes of Ludger, published in IPI of Autumn 2009, it is shown how both the original drug manufacturers and the designers of follow-on biologics could produce biobetter monoclonal antibodies (MAbs) through glycoengineering. (see also Modify Fc fucosylation and β-galactosylation for biobetter MAbs, Design out NeuGc, Fab glycosylation for biobetter MAbs, Design out Gal-α(1,3)-Gal for biobetter MAbs, When is a glycoengineered biobetter commercially better than a biosimilar? and Ludger’s GTO-QbD: Defining glycovariant biobetter MAbs)

Ludger’s GTO-QbD: Defining glycovariant biobetter MAbs

One area of great interest to developers, copiers and improvers of therapeutic antibodies is glycosylation, since it can significantly influence the safety and efficacy profiles of the drug. In an article by Claire Morgan and Daryl Fernandes of Ludger published in IPI of Autumn 2009, it is shown how both the original drug manufacturers and the designers of follow-on biologics could produce biobetter antibodies through glycoengineering. In particular, they examine strategies for optimising both fragment antigen-binding (Fab) and fragment crystallisable (Fc) region glycosylation to produce monoclonal antibodies (MAbs) with improved clinical performance and better commercial profiles compared to existing drugs.

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