title: Tryptathionine bridges in peptide synthesis.
abstract: The tryptathionine linkage is a crosslink formed between tryptophan and cysteine. This feature is characteristic of the bicyclic peptides: the phallotoxins and the amatoxins. These peptides both bind to protein folds of their respective targets (F-actin and RNA pol II, respectively) with extremely high affinities. Studies on these peptides have shown that the tryptathionine crosslink is essential for this binding affinity. Tryptathionines have been investigated for many years and several syntheses exist for their formation. In this review, we report on the various methodologies employed in tryptathionine synthesis, and discuss some of the advantages and disadvantages associated with each of them.
authors.affiliation: Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, V6T 1Z1, Canada.
authors.forename: Jonathan P
authors.initials: JP
authors.lastname: May
authors.forename: David M
authors.initials: DM
authors.lastname: Perrin
mesh_terms: D000546:Amanitins / Q000138:chemical synthesis / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D004583:Electrons; D007211:Indoles / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry
chemical_list: D000546:Amanitins; D003432:Cross-Linking Reagents; D007211:Indoles; D010455:Peptides; C018358:phallotoxin; C018207:amatoxin; D014364:Tryptophan; D003545:Cysteine