Inhibition of polymerase activity by pristine fullerene nanoparticles can be mitigated by abundant proteins.
Pristine fullerene nanoparticles are capable of adsorbing polymerase and significantly inhibiting its biologically important replication activity; however, the inhibition can be partially mitigated by abundant proteins through competitive binding.
Maoyong
Song
S
State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing, 100085, China.
Guibin
Jiang
J
Junfa
Yin
Y
Hailin
Wang
W
D001667:Binding, Competitive; D004247:DNA / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000737:chemistry*; D037741:Fullerenes / Q000737:chemistry*; D006801:Humans; D053758:Nanoparticles / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism
D005456:Fluorescent Dyes; D037741:Fullerenes; D011506:Proteins; D012709:Serum Albumin; C530172:pristine (C60); D004247:DNA; D004259:DNA-Directed DNA Polymerase