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. Author manuscript; available in PMC: 2010 Jul 1.

Published in final edited form as: Anal Chem. 2009 Jul 1;81(13):5490–5495. doi: 10.1021/ac900759k

Fluorescence measurements to determine dissociation constants (K_d) of selected aptamers. A) The initial, naïve library exhibits negligible binding to the streptavidin target ). After the first round of selection, the average K_d of the enriched pool was 94 ± 10 nM (■). Subsequently, second and third round selections yielded an average K_d of 62 ± 5 nM () and 33 ± 5 nM (), respectively. B) After a single round of negative selection against BSA, the aptamer pool exhibited slightly higher affinity for streptavidin (K_d = of 30 ± 5 nM, ). In contrast, the affinity for BSA significantly decreased 5-fold from () to ().

Inline graphic — Fluorescence measurements to determine dissociation constants (K_d) of selected aptamers. A) The initial, naïve library exhibits negligible binding to the streptavidin target ). After the first round of selection, the average K_d of the enriched pool was 94 ± 10 nM (■). Subsequently, second and third round selections yielded an average K_d of 62 ± 5 nM () and 33 ± 5 nM (), respectively. B) After a single round of negative selection against BSA, the aptamer pool exhibited slightly higher affinity for streptavidin (K_d = of 30 ± 5 nM, ). In contrast, the affinity for BSA significantly decreased 5-fold from () to ().