Table 1.

Inhibitory constants of β-clamp ligands^a,b,c.

Ligand	Molecule	IC50 (μM)	Ki, d (μM)	Method	References
NATURAL PEPTIDE
Pol IV peptide (P1)	R0Q1L2V3L4G5L6	8.85	0.15	SPR to β-clamp	Wolff et al., 2011
Consensus	Q1L2D3L4F5	63.2	29.5	FP to β-clamp	Yin et al., 2013
MODIFIED PEPTIDES
Ac-consensus	Ac-Q1L2D3L4F5	1.9	0.9	FP to Pol III β-clamp	Yin et al., 2013
Ac-consensus	Ac-Q1L2D3L4F5	0.07	n.r.	α-subunit plate binding	Wijffels et al., 2011
Ac-consensus (P6)	Ac-Q1L2D3L4F5	1.12	1.2	SPR to β-clamp	Wolff et al., 2011
Ac-cons.+diClF5	Ac-Q1L2D3L4(3,4)ClF5	0.021	n.r.	α-subunit plate binding	Wijffels et al., 2011
P14	Ac-Q1Cha2D3L4(3,4)ClF5	0.077	i, 17	SPR to β-clamp	Wolff et al., 2011
SMALL MOLECULES
RU-7	RU-7	n.r.	i, 10	Pol III replication assay	Georgescu et al., 2008
O-8	compound 8	115	i, 64	screen, x-ray structure	Yin et al., 2014a
Compound 4	compound 4	40	n.r.	α-subunit plate binding	Wijffels et al., 2011
NATURAL PRODUCT
CGM	Pro-8-cylohexanyl GM	n.r.	0.66	SPR	Kling et al., 2015

^aFP, fluorescence polarization; SPR, surface plasmon resonance.

^bn.r., value not reported.

^cDissociation constants are reported in the original literature sometimes as Ki and in others as Kd. Kd's are listed except where noted as Ki.