Fig. 2: Two disulfide bonds formation in α-conotoxin. | Nature Communications

Fig. 2: Two disulfide bonds formation in α-conotoxin.

From: General synthetic strategy for regioselective ultrafast formation of disulfide bonds in peptides and proteins

Fig. 2

a HPLC-ESI MS analyses: Reaction at time zero, the main peak corresponds to reduced α-conotoxin peptide modified with two Acm groups at Cys (2&7) with the observed mass 1499.2 ± 0.1 Da, calcd. 1499.6 Da (average isotopes). b Reaction after 10 s: the main peak corresponds to α-conotoxin peptide bearing one disulfide bond modified with two Acm groups at Cys (2&7) with the observed mass 1497.2 ± 0.1 Da, calcd. 1497.6 Da (average isotopes). c In situ addition of 15 equiv. PdCl2 for 5 min followed by DTC/DSF treatment: the main peak corresponds to α-conotoxin peptide bearing two disulfide bonds with the observed mass 1352.6 ± 0.1 Da, calcd. 1353.6 Da (average isotopes). d Purification and folding: the main peak corresponds to α-conotoxin peptide bearing two disulfide bonds with the observed mass 1352.6 ± 0.1 Da, calcd. 1353.6 Da (average isotopes). e commercially available native α-conotoxin with the observed mass 1352.8 ± 0.1 Da, calcd. 1353.6 Da (average isotopes) (f) synthetic α-conotoxin CD spectrum.

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