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. Author manuscript; available in PMC: 2010 Mar 25.
Published in final edited form as: Angew Chem Int Ed Engl. 2009;48(46):8712–8715. doi: 10.1002/anie.200904550

Table 1.

Amino acid sequences of apamin, PMI, and stingins and their dissociation equilibrium constants for p53-binding domains of MDM2 and MDMX. Each Kd value is the mean of three independent measurements (N.B. = no binding).

Name Sequence Kd (nM)

MDM2 MDMX
Apamin graphic file with name nihms185660t1.jpg N.B. N.B.
PMI 3.2 ± 1.1 8.5 ± 1.7
Stingin-1 CNCKAPETFLCYWRCLQH 25.1 ± 5.1 11.4 ± 2.3
Stingin-2 CNCKAPETFLCYWRCLQ 35.2 ± 3.7 18.0 ± 2.3
Stingin-3 CNCKAPETFLCYWRCL 57.5 ± 7.2 16.0 ± 4.5
Stingin-4 CNCKAPETAFCAYWCQLH 83.2 ± 8.4 252 ± 23
Stingin-5 CNCKAPETAFCAYWCQL 17.7 ± 4.0 93.4 ± 9.2