246855-74-3Relevant academic research and scientific papers
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 (2008/02/09)
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.
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.
