Fig. 1: Interchain disulfide pairing chemistry for peptide heterodimerizations. | Nature Communications

Fig. 1: Interchain disulfide pairing chemistry for peptide heterodimerizations.

From: De novo design and directed folding of disulfide-bridged peptide heterodimers

Fig. 1

a SeCys-mediated thiol-disulfide exchanges between Cys and Pen residues to direct the heterodimerization of peptides with multiple disulfide bonds. b HPLC chromatograms showing the oxidation of 1 (0.1 mM; sequence: WGCGKG3CG) and 2 (0.2 mM; sequence: WGPenGKG3PenG) in the presence of SeCys (0.05 mM) in a phosphate buffer (100 mM, pH 7.4); left: before oxidation, right: after 24 h oxidation. Other peaks in HPLC: 2-SeCys, peptide 2 linked with one SeCys; 2-SeCys2, peptide 2 linked with two SeCys; c1: disulfide-cyclic 1; c2, disulfide-cyclic 2. c HPLC chromatograms showing the oxidation of 2 (0.2 mM) and 3 (0.1 mM; sequence: WGCG2KG2CGKG3PenGKG3CGW) in a phosphate buffer (100 mM, pH 7.4) containing 0.05 mM SeCys and the oxidation of 4 (0.1 mM; sequence: WGCG2KG2CGKG3CGKG3CGW) and 1 (0.2 mM) under the same condition. Source data are provided as a Source Data file.

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