10.1021/tx300289d.s001 V. G. Vaidyanathan V. G. Vaidyanathan Lifang Xu Lifang Xu Bongsup P. Cho Bongsup P. Cho Binary and Ternary Binding Affinities between Exonuclease-Deficient Klenow Fragment (Kf-exo<sup>–</sup>) and Various Arylamine DNA Lesions Characterized by Surface Plasmon Resonance American Chemical Society 2012 surface plasmon resonance KD values Surface Plasmon ResonanceWe dCTP FABP SPR Various Arylamine DNA Lesions Characterized dG adducts FAF arylamine carcinogens Ternary Binding Affinities koff FAAF Tight polymerase binding Klenow binding interactions 2012-08-20 00:00:00 Journal contribution https://acs.figshare.com/articles/journal_contribution/Binary_and_Ternary_Binding_Affinities_between_Exonuclease_Deficient_Klenow_Fragment_Kf_exo_sup_sup_and_Various_Arylamine_DNA_Lesions_Characterized_by_Surface_Plasmon_Resonance/2495152 We used surface plasmon resonance (SPR) to characterize the binding interactions between the exonulease-free Klenow fragment (Kf-exo<sup>–</sup>) and unmodified and modified dG adducts derived from arylamine carcinogens: fluorinated 2-aminofluorene (FAF), 2-acetylaminofluorene (FAAF), and 4-aminobiphenyl (FABP). Tight polymerase binding was detected with unmodified dG and the correct dCTP. The discrimination of correct versus incorrect nucleotides was pronounced with <i>K</i><sub>D</sub> values in the order of dCTP ≪ dTTP < dATP < dGTP. In contrast, minimal selectivity was observed for the modified templates with Kf-exo<sup>–</sup> binding tighter to the FAAF (<i>k</i><sub>off</sub>: 0.02 s<sup>–1</sup>) and FABP (<i>k</i><sub>off</sub>: 0.01 s<sup>–1</sup>) lesions than to FAF (<i>k</i><sub>off</sub>: 0.04 s<sup>–1</sup>).