Synthetic Routes to Thiooligosaccharides and Thioglycopeptides

Dechalcogenative Allylic Selenosulfide and Disulfide Rearrangements: Complementary Methods for the Formation of Allylic Sulfides in the Absence of Electrophiles. Scope, Limitations, and Application to the Functionalization of Unprotected Peptides in Aqueous Media.

“…1,2,17 Native chemical ligation (NCL) for the synthesis of peptides and proteins, and its enzyme-promoted biochemical equivalent, expressed protein ligation, [18][19][20][21] is one such reaction that takes advantage of the sulfhydryl group and which uses it to great advantage in the highly chemoselective formation of amide bonds in aqueous solution. 10,[21][22][23][24][25][26][27][28][29][30][31] Another thiol-based method, the selective formation of mixed disulfides, is both one of the oldest and most enduring of ligation methods.…”

“…1,2,[32][33][34][35][36][37][38] The mildness of the disulfide ligation and its established chemoselectivity for the cysteine thiol in the presence of all the proteinogenic amino acids stands in stark contrast to the various other methods for cysteine functionalization, most of which involve the capture of the cysteine thiol by electrophilic species, and which consequently have obvious potential chemoselectivity issues. 1,2,39 The practicality of the disulfide ligation, with its direct applicability to cysteine-containing peptides, also contrasts with the various ingenious indirect methods that have been developed for the preparation of S-functionalized cysteine derivatives, 17 including, for example, the Michael addition of thiols to dehydroalanine units, 40 the alkylation of thiolates with peptide-based β-halo-alanine units, [41][42][43] and other electrophiles, 44,45 the opening of peptide-based aziridines by thiolates, 46,47 and the synthesis of peptides with previously functionalized cysteine building blocks, [48][49][50] each of which requires the synthesis of modified peptides. The many advantages of the disulfide ligation are offset, however, by its impermanence, which results from the lability of the disulfide bond in the presence of thiols and other reducing agents.…”

Chemo-enzymatic synthesis of an original arabinofuranosyl cluster: optimization of the enzymatic conditions

“…However, this binding affinity increases synergistically with an increasing number of sugar residues: such phenomena, noted by Lee and co-workers in 1995, are often referred to as Thioglycosidic bonds are of great importance in biomolecules and their analogues as their incorporation has led to more stable glycomimetics with potential drug activities. 10 Until now only chemical methods were available for their incorporation into glycofuranosyl conjugates. 11 However, enzymatic strategies are becoming an emerging area as notably envisioned by Prof.…”

Synthesis and Application of Glycopeptide and Glycoprotein Mimetics

“…The preparation of S-linked glycopeptides/proteins has been covered by several excellent reviews [23,32,38,71], most notably a very recent one by Pachamuthu and Schmidt [28]. The present article, therefore, will focus on selected examples.…”

“…This article summarizes recent progress in the field of synthetic glycosylated amino acids, peptides, and proteins with non-natural structural elements, with a focus on the carbohydratepeptide linkage. For a more complete coverage of this wide area, the reader is referred to other excellent reviews [23,[28][29][30][31][32][33][34][35][36][37][38].…”