Disulfide bond formation in peptides.
The formation of disulfide bridges is often a crucial final stage in peptide synthesis. There is compelling evidence that the disulfide pattern can be critical in the folding and structural stabilization of many natural peptide and protein sequences, while the artificial introduction of disulfide bridges into natural or designed peptides may often improve biological activities/specificities and stabilities. This unit provides a highly selective, albeit state-of-the-art, menu of procedures that can be performed to establish intramolecular or intermolecular disulfide bridges in targets of varying complexities.
Chen
Lin
L
AxCell Biosciences Corporation, Newtown, Pennsylvania.
Annis
Ioana
I
Union Carbide Corporation, Bound Brook, New Jersey.
Barany
George
G
University of Minnesota, Minneapolis, Minnesota.
D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry*; D005292:Ferricyanides / Q000737:chemistry; D005978:Glutathione / Q000737:chemistry; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
D004220:Disulfides; D005292:Ferricyanides; D010455:Peptides; D005978:Glutathione; D003545:Cysteine; C028033:potassium ferricyanide