%0 Journal Article
%A Vaidyanathan, V. G.
%A Xu, Lifang
%A Cho, Bongsup P.
%D 2012
%T Binary and Ternary Binding
Affinities between Exonuclease-Deficient
Klenow Fragment (Kf-exo–) and Various Arylamine
DNA Lesions Characterized by Surface Plasmon Resonance
%U 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
%R 10.1021/tx300289d.s001
%2 https://ndownloader.figshare.com/files/4138027
%K surface plasmon resonance
%K KD values
%K Surface Plasmon ResonanceWe
%K dCTP
%K FABP
%K SPR
%K Various Arylamine DNA Lesions Characterized
%K dG adducts
%K FAF
%K arylamine carcinogens
%K Ternary Binding Affinities
%K koff
%K FAAF
%K Tight polymerase binding
%K Klenow
%K binding interactions
%X We used surface plasmon resonance (SPR) to characterize
the binding
interactions between the exonulease-free Klenow fragment (Kf-exo–) 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 KD values in the order of dCTP ≪ dTTP < dATP
< dGTP. In contrast, minimal selectivity was observed for the modified
templates with Kf-exo– binding tighter to the FAAF
(koff: 0.02 s–1) and
FABP (koff: 0.01 s–1) lesions than to FAF (koff: 0.04 s–1).
%I ACS Publications