Journal
CHEMICAL RESEARCH IN TOXICOLOGY
Volume 25, Issue 8, Pages 1568-1570Publisher
AMER CHEMICAL SOC
DOI: 10.1021/tx300289d
Keywords
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Funding
- NCI/NIH [CA098296]
- NCRR/NIH [P20 RR016457]
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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 K-D 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 (k(off): 0.02 s(-1)) and FABP (k(off): 0.01 s(-1)) lesions than to FAF (k(off): 0.04 s(-1)).
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