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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Capítulos
- 00:04Título
- 00:49Solid-Phase Peptide Synthesis (SPPS), Peptide Cleavage from the Resin, and Purification of the Linear Precursor
- 03:04Selective Formation of the Disulfide Bonds
- 04:44Peptide Purification
- 05:56Peptide Analytics
- 08:04MS/MS Analysis of Disulfide Connectivity
- 09:49Results: The Sequential Walk and the Resulting NMR Solution Structure of a Rigid and a Flexible -PIIIa Isomer
- 10:30Conclusion
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.
