Highly Stable Aptamers Selected from a 2'-Fully Modified fGmH RNA Library for Targeting Biomaterials

Friedman A, Kim D, Liu R, 36:110-23, Biomaterials, 2015

This article describes an in vitro selection of fGmH RNA aptamers with enhanced binding affinity and higher specificity to Staphylococcus aureus Protein A (SpA) protein. The study used a 2'-fully modified RNA library (with N40 randomized) transcribed from a dsDNA library by His-tagged LAR T7 RNA polymerase mutant. The data suggest greater stability of RNA aptamers against alkaline hydrolysis and serum nucleases. Additionally these aptamers can perform as SpA affinity-based delivery reagents of antimicrobial agents. Both SPR (Biacore 3000) and BLI (Octet QK) platforms were used in the affinity characterizations. Authors underscore features such as the high throughput nature, enhanced automation, and relatively low cost as reasons for using the Octet platform. An Octet QK equipped with Protein A biosensors were used for affinity measurements. Specificity measurements involved ProA, ProG, and ProL biosensors.

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