. Author manuscript; available in PMC: 2014 Oct 4.

Published in final edited form as: Chem Commun (Camb). 2013 Oct 4;49(76):8543–8545. doi: 10.1039/c3cc44569k

Table 1.

SPR analysis of kinetic rate constants and equilibrium affinities for KA1039 binding to its cognate site TGGCTT^a

			K_d (nM)
[NaCl]	k_a (×10⁶ M⁻¹s⁻¹)	k_d (×10⁻³ s⁻¹)	Kinetic fit	Steady state
50 mM	7.1 ± 0.8	26 ± 2	3.7 ± 0.4	4.0 ± 0.2
100 mM	4.5 ± 0.9	29 ± 3	6.5 ± 0.6	6.3 ± 0.6
200 mM	2.4 ± 0.2	32 ± 6	13 ± 1.1	13 ± 0.5
300 mM	1.5 ± 0.2	33 ± 4	22 ± 0.3	21 ± 1.0

Kinetic analysis was performed by global fitting of 1:1 binding model: k_a=(d[AB]/dt)/([A]*[B]), k_d=(−d[AB]/dt)/[AB] and K_d=k_d/k_a, where [A], [B] and [AB] are the concentrations of the immobilized DNA, PA, and complex, respectively. Errors listed are the standard errors for the global fit.