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

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

Article DOI: 10.3791/58368-v • 11:44 min • October 2nd, 2018
October 2nd, 2018 •
*1, *1, *1, 1
1Pharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn
* These authors contributed equally

챕터

요약
Automatic Translation

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.

Tags

Peptide Synthesis Disulfide Rich Peptides Disulfide Bridge Pattern Selective Synthesis Chemical Characterization Structural Characterization Solid-phase Peptide Synthesis Resin Cleave Peptide Side Chain Protection Scavenger Mixture Trifluoroacetic Acid
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