Table 2.

Comparative binding affinities and net charge of optimized SAH-MS1-2 peptides

PeptideSequence*IC50Mcl-1, nMIC50p, nM+/−
234
abcdefgabcdefgabcdefga
SAH-MS1-2IWBXQGLXRLGDEINAYYARR90 ± 6>5,000+1
SAH-MS1-10IWBXQGLXRLGDEINAYYAR105 ± 16>5,0000
SAH-MS1-11EIWBXQGLXRLGDEINAYYAR60 ± 5>5,000−1
SAH-MS1-12EIWBXQGLXRLGDEINAYYA84 ± 8>5,000−2
SAH-MS1-13IWBXQELXRLGDEINAYYARR55 ± 5>5,0000
SAH-MS1-14IWBXQSLXRLGDEINAYYARR80 ± 5>5,000+1
SAH-MS1-15IWBXQSLXRLGDEINAYYAR180 ± 13>10,0000
SAH-MS1-16IWBXQELXRLGDEINAYYAR64 ± 6>5,000−1
SAH-MS1-17IWBXQGLXRLGDEINARYAR87 ± 5>5,000+1
SAH-MS1-18IWBXQELXRLGDEINARYAR25 ± 7>5,0000
  • * Mutated residues are indicated in bold.

  • Binding experiments and abbreviations are as in Table 1.

  • The +/− column indicates formal net charge based on standard titration states of residues at pH 7. B, norleucine; X, (S)-4-pentenylalanine;