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. Author manuscript; available in PMC: 2011 Aug 15.
Published in final edited form as: Bioorg Med Chem. 2010 Jun 22;18(16):6099–6108. doi: 10.1016/j.bmc.2010.06.053

Table 3.

ELISA-generated Hdmx inhibition data for the derivatives of the CDLRWF lead and the control p53 peptide.

Compound Name % inhibition at 320 μM IC50 (μM)a
1 p53 (17–26) b 98 ± 2 8 ± 1
4a Boc–WF–NH2 No Inhibition ND c
4b Boc–WF–N(CH2)5 13 ± 1 ND c
5a Boc–RWF–NH2 No Inhibition ND c
5b Boc–RWF–N(CH2)5 42 ± 3 463 ± 45
6a Boc–LRWF–NH2 14 ± 2 ND c
6b Boc–LRWF–N(CH2)5 82 ± 4 192 ± 27
7a Boc–DLRWF–NH2 No Inhibition ND c
7b Boc–DLRWF–N(CH2)5 13 ± 1 ND c
8 c-(ADLRWF) 12 ± 1 ND c
a

Calculated from weighted non-linear fits of dose-dependent responses (see Supporting Information for details).

b

KD of 1 has been reported to be 390 ± 20 nM (ref. 34).

c

Not determined due to low activity and poor solubility at high concentrations.