Table 2. Summary of biophysical data.

Peptide(s)	Schematic	MRE222 a (deg cm2 dmol res–1), (% helicity)68	T M b (°C)	Oligomer state c	IC50 MCL-1/BID (μM)
CC-Di		–31.650 (90%)	75	1.96	No response
CC-Di_S		–30.930 (88%)	53	1.74	26 ± 1
CC-Di_E1		–28.259 (81%)	48	1.93	0.7 ± 0.05
CC-Di_E2		–23.091 (66%)	30	1–2 d	0.09 ± 0.005
CC-Di-A		–6577 (19%)	NA (<0)	NA	No response
CC-Di-A_S		–4910 (14%)	NA (<0)	NA	21 ± 0.4
CC-Di-B		–25.088 (71%)	38	ND	No response
CC-Di-B_S		–16.247 (46%)	27	ND	No response
CC-Di-A + CC-Di-B		–29.154 (82%)	91	ND	Not tested
CC-Di-A_S + CC-Di-B		–27.395 (78%)	74	1.83	44 ± 1
CC-Di-A + CC-Di-B_S		–24.490 (69%)	71	1.9	40 ± 2

^aMean residue ellipticity values at 222 nm from circular dichroism (CD) spectra recorded at 20 °C in PBS at 50 μM of each peptide.

^bMidpoints of thermal denaturation curves determined by monitoring the MRE₂₂₂ between 5 and 90 °C ramped at 40 °C h^–1.

^cOligomeric states determined by analytical ultracentrifugation and expressed relative to monomer molecular mass.

^dData for CC-Di_E2 were fitted to monomer–dimer equilibrium.