Paper Report for: Mahlknecht_2015_Biochem.Biophys.Res.Commun_465_218
Reference
Title: Multimerization of ERBB2/HER2 specific aptamer leads to improved receptor binding Mahlknecht G, Maron R, Schechter B, Yarden Y, Sela M Ref: Biochemical & Biophysical Research Communications, 465:218, 2015 : PubMed
Aptamers represent a promising new treatment modality for cancer. Specificity and high affinity are two parameters that characterize aptamers. In this work, we elucidated physicochemical parameters of an ERBB2/HER2 specific aptamer and determined an optimal multimerization state, leading to higher binding and improved avidity. We applied biochemical, immunochemical and biophysical methodologies to characterize binding behaviors of multimerized versions of an ERBB2/HER2 specific aptamer and demonstrate structural integrity. Finally, we show that the trimeric ERBB2/HER2 specific aptamer instigates no immunogenic response in vivo. In summary, the set of methodologies we employed establishes a way to enhance activity of a model HER2-aptamer.
        
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Mahlknecht G, Maron R, Schechter B, Yarden Y, Sela M (2015) Multimerization of ERBB2/HER2 specific aptamer leads to improved receptor binding Biochemical & Biophysical Research Communications465: 218-24
Mahlknecht G, Maron R, Schechter B, Yarden Y, Sela M (2015) Biochemical & Biophysical Research Communications465: 218-24