(a) Displacement
of intercalated EB from ctDNA by 3 studied by emission
spectroscopy (298 K, pH 7.0, 15% DMSO-TRIS/HCl
buffer, 15 μM ctDNA, 15 μM EB). Inset: determination of
[3] at 50% loss of EB fluorescence (C50); C50 is used to determine
the ctDNA affinity constant, KA, of 3. (b) Graph of KA for 1, 2a, and 3–5 as a
function of the steric bulk of the macrocycle’s alkyl bridge
and the hydrophobicity of the Au3+ complex, log(Po/w) (Table S3).
The surface is the best-fit bivariate linear regression function to
the data. (c) EMSA of selected compounds with supercoiled (SC, form
I) pHOT1 plasmid DNA (DNA, 31.3 ng/well; TBE buffer, pH 7.8); some
nicked-open circular (NOC, form II) DNA is present. The lanes contain
pHOT1 plasmid DNA (lane 1), increasing concentrations of EB (lanes
2–4), 1 (lanes 5–9), 6 (lanes
10–12), and 7 (lanes 13–15). The data prove
that Au3+ is essential for DNA binding. (d) Two- and three-dimensional
deconvolution of the DNA bands in lanes 5–8 of the EMSA gel
shown in Part (c).