This study explores a scaffold-based approach to enhance aptamer-protein complex stability by reducing high dissociation rates (k-off) in aqueous environments. Using TBA15 and TBA22 aptamers for thrombin, a spider-like scaffold enables sandwich binding, improving complex stability. The scaffold’s extremities are modified for functionalization with hydrophobic moieties. Electrophoretic Mobility Shift Assay (EMSA) will assess binding efficiency, offering a promising strategy for more stable aptamer-based applications.

Мустафа А., Эльдиб А.А. (науч. рук. Колпащиков Д.М.) Improving aptamer affinity for tight binding human thrombin // Сборник тезисов докладов конгресса молодых ученых. Электронное издание. – СПб: Университет ИТМО, [2025]. URL: https://kmu.itmo.ru/digests/article/15733