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. Author manuscript; available in PMC: 2026 Jan 15.
Published in final edited form as: Cancer Res. 2025 Jul 15;85(14):2714–2725. doi: 10.1158/0008-5472.CAN-24-4039

Figure 2. Characterization of L-Gln-binding aptamers.

Figure 2.

A. Short complementary oligonucleotides were used to identify the L-Gln binding pocket through nanogolds binding assay. Colorimetric changes of the nanogolds due to oligonucleotide interruption of the 56merA15/L-Gln interaction were measured. B. 67mer-A15, 60mer-A15, 56merA15 and mut56merA15 L-Gln binding kinetics (KD) were calculated by gold nanoparticle-based colorimetric assay. C. Fluorescent intercalator displacement (FID) assay was used to determine the kinetics of L-Gln binding to 56merA15 and mut56merA15 in the indicated timescale. D. Internalization kinetics (Kint) of [3H]-labeled L-Gln was determined in the context of increasing concentrations of 56merA15. Data analyzed using two-tailed t test and standard deviation with statistical significance, ** P < 0.01, *** P < 0.001.