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Double quick, double click reversible peptide “stapling”

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Fig. 2Reversible constraining reaction sequence for peptides 1–3a–d: conditions for conversion from the oxidised state (OX) through theintermediate reduced state (RED) to the constrained peptide (STA) andvice versa (LHS); HRMS analyses of reaction mixture for reversibleinterconversion between 1b and 3b (relevant masses are indicated inblack for the peptide and in green for excess glutathione used duringunconstraining) (RHS).
Fig. 3Analyses on BID derived peptides50 mM phosphate bu 1a,b and 3a,b. (a) Circulardichroism spectra (water/30% acetonitrile); (b) trypsin proteolysis ina 1 : 10 000 enzyme/substrate ratio (50 mM phosphate buffer,200 mM NaCl, pH 7.50); (c) fluorescence anisotropy competition assayfor inhibition of the FITC-BID/Mcl-1 interaction (25 nM tracer, 150 nMprotein, 50 mM Tris buffer, 150 mM NaCl, 0.61% of Triton X-100, pH7.40); (d) fluorescence anisotropy competition assay for inhibition ofthe BODIPY-BAK/Bcl-xL interaction (25 nM tracer, 150 nM protein,ffer, 200 mM NaCl, 0.02 mg mL�1 BSA, pH 7.50).
Fig. 5Biophysical and bioactivity analyses of WT-S and S derivedTFE); (b) RNA degradation assay showing the restoration of S proteinactivity

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