A Saxitoxin-Binding Aptamer with Higher Affinity and Inhibitory Activity Optimized by Rational Site-Directed Mutagenesis and Truncation

Zheng X, et al., 101:41-7, Toxicon, 2015

This study focuses on a previously selected DNA aptamer (APTSTX1) against a toxin know as saxitoxin (STX). Using site-directed mutation and truncation, the authors revealed an aptamer (M-30f) with a 30-fold higher affinity and with better inhibitory properties. Subsequent to optimization, the interaction was monitored through Bio-Layer Interferometry (BLI), ELISA, cell, and mouse bioassays. An Octet RED96 system equipped with super Streptavidin biosensors was used to capture biotinylated aptamers. Varying concentrations of STX subjected to binding with immobilized aptamers revealed precise kinetic parameters.

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