What's New

Government of Canada Invests in Scientific and Clinical Hub for Orphan Drug Development

AGADA is excited to continue collaborations with Dalhousie University researchers and clinicians at the IWK on this 5 year project focusing on enabling drug development for orphan diseases in Nova Scotia.

 

http://www.cbc.ca/news/canada/nova-scotia/dalhousie-university-rare-diseases-cure-zebrafish-acoa-1.3760293

Check out AGADA's new student testimonial page!

Click here to see AGADA's previous research interns and read about their work experiences: AGADA Student Testimonials

Nova Scotia Economic and Rural Development and Tourism

 

 

 

 

 

 

 

 

 

We were delighted to have Minister Michel Samson come to visit our lab and speak about the Global Business Accelerator Program!

https://www.facebook.com/media/set/?set=a.10152813883912264.1073742013.161817467263&type=1

Chronicle Herald, Nova Scotia

 

 

 

 

 

 

 

 

 

 

AGADA Biosciences was recently featured in the business section of the Chronicle Herald Newspaper. http://thechronicleherald.ca/business/1205462-nice-mouse-facilities-at-dal-clinch-deal-for-bioscience-firm.

Intellectual Property

Stable isotope labeling of amino acids in mammals (SILAM) is an approach in which a mammal (e.g., mice) is fed amino acids labeled with stable heavy isotopes (Rayavarapu et al. 2013). These heavy isotopes are incorporated into all the proteins of the animal. The proteins from normal and diseased mice can be combined and analyzed together by mass spectrometry. The identical pair of peptides of different stable-isotope composition can be differentiated based on their mass difference. The ratio of peak intensities for such peptide pairs reflects the abundance ratio of the two proteins. This technique can be used to accurately detect and quantitatively compare the protein abundance in normal and diseased/treated samples using only small amounts of total protein extract. This assay displays the features of a robust surrogate biomarker sought for Phase 2 trials focused on dystrophin replacement in DMD.

 

Application of this approach for quantitative assays for surrogate biochemical outcome measures is being developed by AGADA (patent pending) (Brown et al. 2012).  

  

References:

Brown, K.J., Marathi, R., Fiorillo, A.A., Ciccimaro, E.F., Sharma, S., Rowlands, D.S., Rayavarapu, S., Nagaraju, K., Hoffman, E.P. and Hathout, Y. (2012) Accurate Quantitation of Dystrophin Protein in Human Skeletal Muscle Using Mass Spectrometry. Journal of bioanalysis & biomedicine, Suppl 7. Publication

 

Rayavarapu, S., Coley, W., Cakir, E., Jahnke, V., Takeda, S., Aoki, Y., Grodish-Dressman, H., Jaiswal, J.K., Hoffman, E.P., Brown, K.J. Hathout, Y. and Nagaraju, K. (2013) Identification of disease specific pathways using in vivo SILAC proteomics in dystrophin deficient mdx mouse. Molecular & cellular proteomics: MCP, 12, 1061-1073. Publication


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