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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

DOI :

10.3791/58368-v

October 2nd, 2018

October 2nd, 2018

12,060 Views

1Pharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn

Cysteine-rich peptides fold into distinct three-dimensional structures depending on their disulfide connectivity. Targeted synthesis of individual disulfide isomers is required when buffer oxidation does not lead to the desired disulfide connectivity. The protocol deals with the selective synthesis of 3-disulfide-bonded peptides and their structural analysis using NMR and MS/MS studies.

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