. 2020 Jul 6;6(7):1223–1230. doi: 10.1021/acscentsci.0c00049

Table 1. Comparison of Native MS Data on Ternary Complex Formation with Literature Values.

		K_D of VCB binding to [PROTAC + substrate]		cooperativity	t_1/2 of ternary complex	fraction of ternary complex
PROTAC	substrate	ITC¹⁸	SPR¹⁶	SPR¹⁶	SPR¹⁶	nMS
AT1	Brd4^BD1	390 nM	578 nM	0.2	<1 s	0.65 ± 0.1
AT1	Brd3^BD2	79 nM	163 nM	0.7	3 s	0.58 ± 0.07
AT1	Brd4^BD2	46 nM	24 nM	4.7	26 s	0.82 ± 0.06
MZ1	Brd4^BD1	28 nM	30 nM	0.9	<1 s	0.80 ± 0.06
MZ1	Brd3^BD2	7 nM	8 nM	3.6	6 s	0.83 ± 0.05
MZ1	Brd4^BD2	4 nM	1 nM	22	130 s	0.92 ± 0.03