Proximity-driven site-selective conjugation of aptamers to proteins using deoxy-oxanosine
발표자
김용환 (포항공과대학교)
연구책임자
오승수 (포항공과대학교)
공동저자
김용환 (포항공과대학교), 오승수 (포항공과대학교)
초록
내용
In protein engineering, precise conjugation of nonprotein entities to defined sites on proteins is essential for applications such as antibody–drug conjugates, diagnostics, and targeted delivery. Here, we developed a unique chemical conjugation platform by introducing a deoxyguanosine analogue, deoxyoxanosine (dOxa), into a protein-specific aptamer. Upon target binding, the dOxa-modified aptamer forms a selective and irreversible covalent bond with a nearby lysine on the protein. Using the Tet repressor (TetR) bound to DNA and RNA aptamers, we demonstrated efficient covalent conjugation in a proximity-dependent manner. We further plan to evaluate the functional consequences of this conjugation in TetR-expressing bacteria treated with tetracycline, highlighting the potential of this platform for synthetic biology applications.