Rational peptide design for inhibition of the kix-mll interaction

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SUMMARY

    The average and minimum of the dG_separated values for each mutant were compared with those of the wild_type (Fig 2). The authors evaluated the helical propensity of the aforementioned 24 mutants using the AGADIR ­server27-30 and selected the mutants with a helical propensity higher than that of the wild_type. Of the 11 designed peptides, three peptides with either the K2855R, T2857L, or T2857W mutation exhibited a higher KIX-binding affinity than the wild_type, with a Kd of 1.5 ± 0.1 μM, 1.9 ± 0.1 μM, and 0.95 ± 0.04 μM . . .

     

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