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. Author manuscript; available in PMC: 2011 Nov 24.
Published in final edited form as: Chem Biol. 2010 Nov 24;17(11):1201–1211. doi: 10.1016/j.chembiol.2010.09.011

Figure 2. TcdB CPD rational inhibitor design and screening.

Figure 2

(A) Conserved substrate autocleavage site of C. difficile TcdB and related bacterial toxins. The toxin CPD cleaves after the highlighted leucine residue.

(B) Focused screen of capped di- and tripeptide covalent TcdB CPD inhibitors. Observed IC50 values were determined using the autocleavage assay for covalent AOMK inhibitors with diverse P2 (left) and P3 (right) residues. These compounds were N-terminally capped with carboxybenzyl (Cbz), acetyl (Ac), or hydroxyphenyl acetyl (Hpa) groups. The dipeptide inhibitor Hpa-SL-AOMK was found to be the most potent compound. Data represents the mean of three experiments ± standard deviation.

See also Figure S1.