4229-38-3Relevant academic research and scientific papers
Rapid glycoconjugation with glycosyl amines
Baudendistel, Oliver R.,Rapp, Mareike A.,Steiner, Ulrich E.,Wittmann, Valentin
, p. 14901 - 14906 (2021/12/02)
Conjugation of unprotected carbohydrates to surfaces or probes by chemoselective ligation reactions is indispensable for the elucidation of their numerous biological functions. In particular, the reaction with oxyamines leading to the formation of carbohydrate oximes which are in equilibrium with cyclic N-glycosides (oxyamine ligation) has an enormous impact in the field. Although highly chemoselective, the reaction is rather slow. Here, we report that the oxyamine ligation is significantly accelerated without the need for a catalyst when starting with glycosyl amines. Reaction rates are increased up to 500-fold compared to the reaction of the reducing carbohydrate. For comparison, aniline-catalyzed oxyamine ligation is only increased 3.8-fold under the same conditions. Glycosyl amines from mono- and oligosaccharides are easily accessible from reducing carbohydrates via the corresponding azides by using Shoda's reagent (2-chloro-1,3-dimethylimidazolinium chloride, DMC) and subsequent reduction. Furthermore, glycosyl amines are readily obtained by enzymatic release from N-glycoproteins making the method suited for glycomic analysis of these glycoconjugates which we demonstrate employing RNase B. Oxyamine ligation of glycosyl amines can be carried out at close to neutral conditions which makes the procedure especially valuable for acid-sensitive oligosaccharides. This journal is
Total Synthesis of Glycosylated Human Interferon-γ
Ashhurst, Anneliese S.,Dowman, Luke J.,Fairbanks, Antony J.,Kwan, Ann,Larance, Mark,Li, Henry Y.,Payne, Richard J.,Wang, Xiaoyi,Watson, Emma E.
supporting information, p. 6863 - 6867 (2020/09/15)
Interferon-γ(IFN-γ) is a glycoprotein that is responsible for orchestrating numerous critical immune induction and modulation processes and is used clinically for the treatment of a number of diseases. Herein, we describe the total chemical synthesis of homogeneously glycosylated variants of human IFN-γusing a tandem diselenide-selenoester ligation-deselenization strategy in the C- to N-terminal direction. The synthetic glycoproteins were successfully folded, and the structures and antiviral functions were assessed.
A Tripeptide Approach to the Solid-Phase Synthesis of Peptide Thioacids and N-Glycopeptides
Sch?we, Markus Julian,Keiper, Odin,Unverzagt, Carlo,Wittmann, Valentin
, p. 15759 - 15764 (2019/11/19)
A general and robust method for the incorporation of aspartates with a thioacid side chain into peptides has been developed. Pseudoproline tripeptides served as building blocks for the efficient fluorenylmethyloxycarbonyl (Fmoc) solid-phase synthesis of t
N-Linked Glycosyl Auxiliary-Mediated Native Chemical Ligation on Aspartic Acid: Application towards N-Glycopeptide Synthesis
Chai, Hua,Le Mai Hoang, Kim,Vu, Minh Duy,Pasunooti, Kalyan,Liu, Chuan-Fa,Liu, Xue-Wei
supporting information, p. 10363 - 10367 (2016/08/24)
A practical approach towards N-glycopeptide synthesis using an auxiliary-mediated dual native chemical ligation (NCL) has been developed. The first NCL connects an N-linked glycosyl auxiliary to the thioester side chain of an N-terminal aspartate oligopeptide. This intermediate undergoes a second NCL with a C-terminal thioester oligopeptide. Mild cleavage provides the desired N-glycopeptide.
Convergent Synthesis of N-Linked Glycopeptides via Aminolysis of ω-Asp p-Nitrophenyl Thioesters in Solution
Du, Jing-Jing,Gao, Xiao-Fei,Xin, Ling-Ming,Lei, Ze,Liu, Zheng,Guo, Jun
supporting information, p. 4828 - 4831 (2016/10/14)
An efficient N-linked glycosylation reaction between glycosylamines and p-nitrophenyl thioester peptides has been developed. The reaction conditions are mild and compatible with the C-terminal free carboxylic acid group and the unprotected N-linked sialyl
Rapid formation of N-glycopeptides via Cu(II)-promoted glycosylative ligation
Joseph, Ryan,Dyer, Frank Brock,Garner, Philip
, p. 732 - 735 (2013/03/29)
Herein is described the chemoselective Cu(II)-HOBt promoted chemical ligation of glycosylamines and peptide thioacids to give N-glycosylated peptides. The method is distinguished from other chemical approaches to peptide N-glycosylation in that (1) it can be employed in the presence of unprotected N-terminal and Lys side chain amines; (2) it is remarkably fast, going to completion in under 30 min; and (3) it produces glycopeptides without attendant aspartimide formation.
COMPOSITIONS, METHODS OF SYNTHESIS AND USE OF CARBOHYDRATE TARGETED AGENTS
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Page/Page column 13, (2013/02/28)
The invention provides D02S derivatives conjugated to monosaccharide ligands directly or through a linker and optionally chelated to a metal, wherein theD02S derivatives having the following structure: wherein R1', R2' are each independently-OH or -O-alkyl; R1 is a hydrogen, a linker, or a ligand; R3 is a linker and/or a ligand; and n is an integer from 1 to 10; the linker is an amino acid, a peptide, an amino alcohol, a polyethylylene glycol, an alkyl, an alkenyl, an alkynyl, an azide, an aromatic compound, a carboxylic acid, or an ester, the alkyl, alkenyl, or alkynyl is optionally substituted with an alkyl, a halogen, a nitro group, a hydroxyl group, an amino group, or a carboxyl group; the ligand is a GLUT1 targeting moiety.
Mixed SAMs and MALDI-ToF MS: Preparation of N-glycosylamine derivative and thioctic acid methyl ester bearing 1,2-dithiolane groups and detection of enzymatic reaction on Au
Hassan, Hani Mutlak A.,Maltman, Beatrice A.
experimental part, p. 6 - 9 (2012/03/26)
Herein, we report an enzymatic galactosylation reaction of β-glucopyranosylamide 4 and thioctic acid methyl ester 5 bearing 1,2-dithiolane groups to form a new system of mixed self-assembled monolayers (SAMs) on gold. Characterization of the enzymatic activity was conveniently achieved by mass spectrometry.
Synthesis of amino-bridged oligosaccharide mimetics
Neumann, Janna,Thiem, Joachim
scheme or table, p. 900 - 908 (2010/04/23)
Synthesis of amino-bridged oligosaccharides using reductive animation opens rapid access to novel glycomimetic target structures as potential ligands for the receptor protein NKR P1 of natural killer cells. Emphasis was laid on fast and facile synthetic routes. The carbonyl building blocks were easily obtained by oxidation with Dess-Martin periodinane or iodoxybenzoic acid (IBX). For the required amino-function-alized units, reduction of azide precursors was advantageous, and generation of the novel oligosaccharides was achieved by subsequent reductive amination. The target saccharide structures feature a bridging nitrogen atom inserted between two non-anomeric positions as well as including one anomeric position.
Study of on-resin convergent synthesis of N-linked glycopeptides containing a large high mannose N-linked oligosaccharide
Chen, Rui,Tolbert, Thomas J.
experimental part, p. 3211 - 3216 (2010/05/14)
Here we present a convergent on-resin glycosylamine coupling strategy for solid phase N-linked glycopeptide synthesis, and apply it to the synthesis of high mannose containing glycopeptides. In this strategy, the 2-phenylisopropyl protecting group is used as an orthogonal handle to create glycosylation sites on-resin after synthesis of nonglycosylated peptides. In addition to allowing selective deprotection of aspartic acid residues for creation of glycosylation sites, the 2-phenylisopropyl protecting group also efficiently suppresses aspartimide formation during peptide synthesis. The key step of on-resin glycosylamine coupling to an aspartic acid residue was first optimized for a small sugar, N-acetylglucosamine, and then applied to a much larger high mannose oligosaccharide, Man8GlcNAc2. Satisfying coupling yields were obtained for both small and large sugars. The use of on-resin glycosylamine coupling simplifies purification of N-linked glycopeptides, and also allows convenient recovery of unreacted valuable large oligosaccharides. This approach was applied to the solid phase synthesis of glycosylated forms of the 34 amino acid HIV-1 gp41 C34 glycopeptide, which is an HIV-1 entry inhibitor. The HIV-1 entry inhibition assay of synthesized glycopeptides showed the retention of bioactivity of high mannose Man8GlcNAc2-C34.
