Table 1.

SAHB peptides reported by Verdine^[20] and Walensky.^[25]

Compound	Sequence[a]	Helicity [%][b]	K d [nm]
BID BH3	EDIIRNIARHLAQVGDSNLDRSIW	15.7±0.3	269[c]
BID SAHBA	EDIIRNIARHLA*VGD*NLDRSIW	87.5±0.3	38.8[c]
BID SAHBA(G→E)	EDIIRNIARHLA*VED*NLDRSIW	77.8±0.6	483[c]
BID SAHBB	EDIIRNI*RHL*QVGDSNLDRSIW	85.5±1.3	n.d.
BID SAHBC	EDIIRNIA*HLA*VGDSNLDRSIW	59.7±6.5	n.d.
BID SAHBD	EDIIRNIAR*LAQVGD*NLDRSIW	35.6±1.8	n.d.
Mcl‐1 BH3	KALETLRRVGDGVQRNHETAF	18	245±29[d]
Mcl‐1 SAHBA	KALETLR*VGD*VQRNHETAF	62	43±16[d]
Mcl‐1 SAHBB	KAL*TLR*VGDGVQRNHETAF	100[e]	18±4[d]
Mcl‐1 SAHBC	KALETLRRV*DGV*RNHETAF	81	>1000[d]
Mcl‐1 SAHBD	KALETLRRVGDGV*RNH*TAF	91	10±3[d]
Mcl‐1 SAHBE	KALETLRRVGDGVQR*HET*F	68	33±10[d]

[a] ✶: Indicates location of hydrocarbon staple. [b] Determined by circular dichroism. [c] Determined by a Bcl‐2 FP assay; 95 % CI BID BH3 33.5–44.9 nm, BID SAHB_A 244–297 nm, BID SAHB_A(G→E) 434–536 nm. [d] Determined by an Mcl‐1 FP assay; data are the mean±SD performed in at least triplicate; n.d.: not determined. [e] Exceeds calculated ideal value for undecapeptide standard.