A sugar switch for anti-inflammatory antibodies

Article Abstract:

A study suggests that addition of sialic acid to the oligosaccharides on human immunoglobulin G (IgG) molecules enhances their anti-inflammatory activity but might compromise their cytotoxicity, as evidenced in mice by reduced platelet depletion by platelet-specific recombinant monoclonal antibodies (rMAbs). X-ray crystallography reveals multiple noncovalent interactions between the oligosaccharide and the protein, implying that both influence antibody conformation.

Care and treatment, Autoimmune diseases, Monoclonal antibodies, Sialic acids, Structure

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Post-translational modifications in the context of therapeutic proteins

Article Abstract:

An overview of the range of post-translational modifications (PTMs) associated with natural and recombinant therapeutic proteins is presented and the way such modifications might influence the properties of protein drug candidates is discussed. A better understanding of such structural-functional relationships would facilitate the development of second-generation products displaying a PTM profile engineered to optimize therapeutic usefulness.

Methods, Analysis, Glycosylation, Protein research, Post-translational modification

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Biopharmaceutical benchmarks 2006

Article Abstract:

An update on biopharmaceuticals approved during the past three and a half years (from January 2003 to June 2006), examining which types of biopharmaceuticals are launched and for what indications is presented. Overall, some 165 biopharmaceutical products have gained approval, with a market size estimated at some $33 million in 2004 and projected to reach $70 billion by the end of the decade.

Product information, Government regulation, Licensing, certification and accreditation

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