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. Author manuscript; available in PMC: 2009 Sep 28.
Published in final edited form as: Nature. 2007 Nov 29;450(7170):712–716. doi: 10.1038/nature06261

Figure 2. In vitro characterization of activators of human SIRT1.

Figure 2

a, The effect of SIRT1 activators on peptide substrate Km. b, Calorimetric titrations of SIRT1-C—peptide substrate complex with the activator SRT1460. Top panel: heat of binding SRT1460 to enzyme—peptide complex. Bottom panel: integrated fit with a one-site binding model. c, Isobologram analysis of resveratrol versus SRT1720 and SRT1720 versus SRT1460. The experimental data are best fit to the theoretical line of additivity (dashed line). d, SIRT1 N-terminal truncations define the allosteric compound binding site. The ability of resveratrol and SRT1720 to activate SIRT1 was examined against a series of N-terminal deletions in the mass spectrometry assay.