153252-68-7Relevant articles and documents
Carbohydrate-protein interactions by "clicked" carbohydrate self-assembled monolayers
Zhang, Yun,Luo, Sanzhong,Tang, Yijun,Yu, Lei,Hou, Kuang-Yu,Cheng, Jin-Pei,Zeng, Xiangqun,Wang, Peng George
, p. 2001 - 2008 (2006)
A Huisgen 1,3-dipolar cycloaddition "click chemistry" was employed to immobilize azido sugars (mannose, lactose, α-Gal) to fabricate carbohydrate self-assembled monolayers (SAMs) on gold. This fabrication was based on preformed SAM templates incorporated with alkyne terminal groups, which could further anchor the azido sugars to form well-packed, stable, and rigid sugar SAMs. The clicked mannose, lactose, and α-Gal trisaccharide SAMs were used in the analysis of specific carbohydrate-protein interactions (i.e., mannose-Con A; ECL-lactose, α-Gal-anti-Gal). The apparent affinity constant of Con A binding to mannose was (8.7 ± 2.8) × 10 5 and (3.9 ± 0.2) × 106 M-1 measured by QCM and SPR, respectively. The apparent affinity constants of lactose binding with ECL and α-Gal binding with polyclonal anti-Gal antibody were determined to be (4.6 ± 2.4) × 106 and (6.7 ± 3.3) × 106 M-1, respectively by QCM. SPR, QCM, AFM, and electrochemistry studies confirmed that the carbohydrate SAM sensors maintained the specificity to their corresponding lectins and nonspecific adsorption on the clicked carbohydrate surface was negligible. This study showed that the clicked carbohydrate SAMs in concert with nonlabel QCM or SPR offered a potent platform for high-throughput characterization of carbohydrate-protein interactions. Such a combination should complement other methods such as ITC and ELISA in a favorable manner and provide insightful knowledge for the corresponding complex glycobiological processes.
Carbohydrate conjugation through microwave-assisted functionalization of single-walled carbon nanotubes using perfluorophenyl azides
Kong, Na,Shimpi, Manishkumar R.,Ramstr?m, Olof,Yan, Mingdi
supporting information, p. 33 - 38 (2015/03/14)
Carbohydrate-functionalized single-walled carbon nanotubes (SWNTs) were synthesized using microwave-assisted reaction of perfluorophenyl azide with the nanotubes. The results showed that microwave radiation provides a rapid and effective means to covalently attach carbohydrates to SWNTs, producing carbohydrate-SWNT conjugates for biorecognition. The carbohydrate-functionalized SWNTs were furthermore shown to interact specifically with cognate carbohydrate-specific proteins (lectins), resulting in predicted recognition patterns. The carbohydrate-presenting SWNTs constitute a new platform for sensitive protein- or cell recognition, which pave the way for glycoconjugated carbon nanomaterials in biorecognition applications.
Altering Cancer Cellular Functions through Proton Mopping
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Paragraph 0011-0012, (2015/03/16)
Proton mopping is a new anti-cancer therapeutic approach that disrupts cancer's immunologic balance. It results in the alteration of the pHi/pHe ratio (intracellular-extracellular) of the cancer cell, leading cancer to either normalcy or apoptosis. This technology deploys a chemical compound that has two parts, a glucose part to guide the molecule to the cancer site and a proton neutralizer to mop up the protons. Proof of the validity of this therapeutic approach came after using an existing chemical compound 2-[2(2-Aminoethoxy)ethoxy]ethyl a-D-mannopyranoside, C12H25NO8, which has the above mentioned properties. This compound is of the class of functionalized PEGylated glycosides, which are ligands for conjugation to biological molecules.
Stereoselective synthesis of light-activatable perfluorophenylazide- conjugated carbohydrates for glycoarray fabrication and evaluation of structural effects on protein binding by SPR imaging
Deng, Lingquan,Norberg, Oscar,Uppalapati, Suji,Yan, Mingdi,Ramstroem, Olof
experimental part, p. 3188 - 3198 (2011/06/10)
A series of light-activatable perfluorophenylazide (PFPA)-conjugated carbohydrate structures have been synthesized and applied to glycoarray fabrication. The glycoconjugates were structurally varied with respect to anomeric attachment, S-, and O-linked carbohydrates, respectively, as well as linker structure and length. Efficient stereoselective synthetic routes were developed, leading to the formation of the PFPA-conjugated structures in good yields over few steps. The use of glycosyl thiols as donors proved especially efficient and provided the final compounds in up to 70% total yield with high anomeric purities. PFPA-based photochemistry was subsequently used to generate carbohydrate arrays on a polymeric surface, and surface plasmon resonance imaging (SPRi) was applied for evaluation of carbohydrate-protein interactions using the plant lectin Concanavalin A (Con A) as a probe. The results indicate better performance and equal efficiency of S- and O-linked structures with intermediate linker length.
Assessing the cluster glycoside effect during the binding of concanavalin A to mannosylated artificial lipid rafts
Noble, Gavin T.,Flitsch, Sabine L.,Liem, Kwan Ping,Webb, Simon J.
supporting information; experimental part, p. 5245 - 5254 (2010/04/04)
Mannosyl glycolipids with perfluoroalkyl membrane anchors have been synthesised. When inserted into vesicles, these mannosyl lipids either dispersed evenly over the surface or, in the presence of cholesterol, phase-separated into artificial lipid rafts. At 1% mol/mol, the affinity of dispersed mannosyl lipids for Con A was 3-fold weaker than in solution, perhaps reflecting steric blocking by the surface. However increasing membrane loading 5-fold increased Con A affinity by up to 75% and indicated weak intramembrane chelation of Con A. Despite this observation, concentrating the mannosyl lipids into artificial lipid rafts did not significantly improve affinity for Con A. This lack of a cluster glycoside effect was ascribed to lipid congestion inhibiting intra-raft chelation of Con A, and implies that glycolipids located in lipid rafts may not necessarily be preorganised for multivalent binding.
Gold nanoparticle-based competitive colorimetric assay for detection of protein-protein interactions
Tsai, Charng-Sheng,Yu, Ting-Bin,Chen, Chao-Tsen
, p. 4273 - 4275 (2007/10/03)
A gold nanoparticle-based competitive colorimetric assay uses the ensemble of Concanavalin (ConA) and mannopyranoside-encapsulated gold nanoparticles (Man-GNPs) to identify the binding partners for ConA and the binding constants are determined based on the wavelength shifts. The Royal Society of Chemistry 2005.
Bacteria targeted by human natural antibodies using α-gal conjugated receptor-specific glycopolymers
Li, Jun,Zacharek, Sima,Chen, Xi,Wang, Jianqiang,Zhang, Wei,Janczuk, Adam,Wang, Peng George
, p. 1549 - 1558 (2007/10/03)
Synthesis of polymerizable β-lactosyl, Galα1→3Gal and α-mannosyl acrylamide derivatives with either a hydrophobic aromatic spacer or a hydrophilic biocompatible oligoethoxyl spacer was accomplished. Radical terpolymerizations of β-lactosyl monomer, α-mannosyl monomer, and acrylamide were conducted in aqueous media with ammonium persulfate and N,N,N',N'-tetramethylethylenediamine as initiators. The resulting water soluble glycopolymers were further transformed efficiently by a recombinant α1→3 galactosyltransferase to afford mediators bearing Galα1→3Gal termini as xenoactive antigens and α-mannosyl termini as specific ligands for bacterial cells. The binding of the resulting multivalent glycopolymer to bacteria was tested by its ability to inhibit agglutination of yeast to E. coli. The binding of human natural anti-Gal antibodies to the α-Gal containing glycopolymers and a monovalent α-Gal-Man glycoconjugate was demonstrated by an ELISA inhibition assay. Copyright (C) 1999 Elsevier Science Ltd.
