Nuron closing in on new treatment for relapsing MS

A board to discuss future MS therapies in early stage (Phase I or II) trials.

Nuron closing in on new treatment for relapsing MS

Postby MSUK » Wed Nov 14, 2012 3:27 am

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Nuron Biotech Inc. said Tuesday it has completed enrollment of 500 patients for a pivotal phase-III study evaluating the safety and effectiveness of the company’s experimental multiple sclerosis treatment.

Phase-III studies are typically the last hurdle a drug developer must clear before seeking approval for a new drug candidate.

Nuron, an Exton, Pa., specialty biologics and vaccines company, is developing NU100 to treat relapsing remitting multiple sclerosis.

Shankar Musunuri, the company’s founder and CEO, said it expects to complete the study in late 2013.... Read More - http://www.msrc.co.uk/index.cfm/fuseact ... ageid/2872
MS-UK - http://www.ms-uk.org/
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Re: Nuron closing in on new treatment for relapsing MS

Postby NHE » Wed Nov 14, 2012 4:48 am

About NU100
NU100 is a proprietary recombinant human interferon beta-1b produced utilizing proprietary refolding process technology. It is being developed as a standalone molecule for the treatment of relapsing remitting multiple sclerosis (RRMS) and as a new molecular entity based on positive opinion from the European Medicines Agency and the Food and Drug Administration.

Patients treated with currently marketed interferon beta-1b products have up to 40 percent neutralizing antibody prevalence after two years of treatment. NU100 is essentially aggregate-free compared to those products; therefore, it should result in lower immune responses, potentially improving overall long-term clinical efficacy and improving the tolerability and safety for RRMS patients presently requiring therapy with interferon beta-1b.


I think the problem with interferon beta-1b's high rate of antigenicity is the fact that it's produced in bacteria and is therefore not glycosylated (doesn't have any attached sugar groups). In contrast, human interferon beta is glycosylated and is identical to interferon beta-1a. The lack of glycosylation on an otherwise normally glycosylated protein will make the 1b form appear as a foreign protein and increase its antigenicity and its tendency to elicit neutralizing antibodies.

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