Synthesis of a Novel Polyaniline Glycopolymer and its Lectin Binding Studies

2014 ◽  
Vol 67 (4) ◽  
pp. 562 ◽  
Author(s):  
Christopher Wilcox ◽  
Jianyong Jin ◽  
Hayley Charville ◽  
Simon Swift ◽  
Teresa To ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Concanavalin A ◽  
Lectin Binding ◽  
Water Soluble ◽  
Binding Studies ◽  
Aniline Derivative ◽  
Selective Binding ◽  
Multistep Synthesis ◽  
Potential Applications ◽  
Mannose Receptors

We report the multistep synthesis and polymerisation of a novel aniline derivative with a pendant α-d-mannose substituent. The α-D-mannose functionality was successfully introduced before polymerisation via copper-catalysed azide alkyne click chemistry and the resulting monomer was polymerised using general oxidative polymerisation conditions, producing a water soluble mannosylated polyaniline. The polymer was characterised by several techniques and compared with standard polyaniline. The selective binding of the polymer to Concanavalin A (ConA) was successfully demonstrated by the precipitation of polymer–ConA aggregates. Potential applications of these novel polyaniline glycopolymers could include the development of electroactive biomaterials with the ability to bind mannose receptors, or as sensors for proteins or microbes.

Effects of bovine serum albumin on the interaction of concanavalin A and succinyl-concanavalin A with phospholipid bilayers

1985 ◽  
Vol 63 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Christina A. Chicken ◽  
Frances J. Sharom
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Concanavalin A ◽  
High Purity ◽  
Binding Sites ◽  
Bovine Serum ◽  
Lectin Binding ◽  
Affinity Column ◽  
Binding Studies ◽  
High Affinity

Under physiological conditions, concanavalin A interacts with the surface of phospholipid liposomes through two distinct classes of binding sites, a relatively small number of high affinity sites and a much larger number of lower affinity sites. Addition of bovine serum albumin induces extensive additional binding of concanavalin A to liposomal membranes and this binding is saturable and "specific" (α-methyl mannoside inhibitable). Fraction V and high purity albumin both induce almost identical levels of concanavalin A binding to liposomes. Scatchard plots of the binding data demonstrate the induction of a large number of new, relatively high affinity lectin-binding sites on addition of albumin. Albumin-induced binding of concanavalin A to the bilayer surface shows a broad pH optimum and is not inhibited by 40% (w/v) ethylene glycol, suggesting that hydrophobic forces are relatively unimportant. In contrast, divalent succinyl-concanavalin A shows very little tendency to bind to liposomes, either in the absence or presence of albumin. Passage of high purity albumin down a concanavalin A affinity column or treatment with periodate completely eliminates the additional lectin binding. It thus seems likely that albumin-induced concanavalin A binding to liposomes is related to the presence of a concanavalin-A-binding component. This phenomenon may have important implications for lectin-binding studies carried out on membranes which have been exposed to serum proteins.

scholarly journals Studies on the cell surface of zoospores and cysts of the fungus Phytophthora cinnamomi: nature of the surface saccharides as determined by quantitative lectin binding studies.

1985 ◽  
Vol 33 (5) ◽  
pp. 384-388 ◽  
Author(s):  
A Bacic ◽  
M L Williams ◽  
A E Clarke
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Phytophthora Cinnamomi ◽  
Lectin Binding ◽  
Soybean Agglutinin ◽  
Binding Studies ◽  
Con A

The nature of the surface saccharides of zoospores, "partially encysted zoospores" and cysts of the root-rotting fungus Phytophthora cinnamomi, has been examined by quantitative lectin binding studies. Zoospores bound concanavalin A (Con A), but did not bind any of a variety of other lectins tested. In contrast, both cysts and "partially encysted zoospores" bound soybean agglutinin (SBA) as well as Con A. This indicates that accessible alpha-D-glucosyl/alpha-D-mannosyl-containing glycoconjugates predominate at the zoospore surface, whereas both alpha-D-glucosyl/alpha-D-mannosyl and galactosyl and/or N-acetyl-D-galactosaminosyl residues are accessible at the surface of cysts and "partially encysted zoospores." Neither Ulex europeus lectin nor wheat germ agglutinin (WGA) bound to any of the three cell preparations, indicating the absence of accessible alpha-L-fucosyl and N-acetyl-D-glucosaminosyl residues.

Lectin Binding Studies on RNA Tumor Virus-Infected Cells

1975 ◽  
Vol 33 ◽  
pp. 326-327
Author(s):  
D. C. Hixson
Keyword(s):  
Binding Sites ◽  
Lectin Binding ◽  
Culture Conditions ◽  
3T3 Cells ◽  
Binding Studies ◽  
Con A ◽  
Microscopic Studies ◽  
Tumor Virus ◽  
Infected Cells ◽  
Cell Culture Conditions

The abilities of plant lectins to preferentially agglutinate malignant cells and to bind to specific monosaccharide or oligosaccharide sequences of glycoproteins and glycolipids make them a new and important biochemical probe for investigating alterations in plasma membrane structure which may result from malignant transformation. Electron and light microscopic studies have demonstrated clustered binding sites on surfaces of SV40-infected or tryp- sinized 3T3 cells when labeled with concanavalin A (con A). No clustering of con A binding sites was observed in normal 3T3 cells. It has been proposed that topological rearrangement of lectin binding sites into clusters enables con A to agglutinate SV40-infected or trypsinized 3T3 cells (1). However, observations by other investigators have not been consistent with this proposal (2) perhaps due to differences in reagents used, cell culture conditions, or labeling techniques. The present work was undertaken to study the lectin binding properties of normal and RNA tumor virus-infected cells and their associated viruses using lectins and ferritin-conjugated lectins of five different specificities.

Facile fractionation of bamboo hydrolysate and characterization of isolated lignin and lignin-carbohydrate complexes

Holzforschung ◽  
2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Xiaodi Wang ◽  
Yongchao Zhang ◽  
Luyao Wang ◽  
Xiaoju Wang ◽  
Qingxi Hou ◽  
...  
Keyword(s):  
Solvent Extraction ◽  
Organic Solvent ◽  
Extraction Process ◽  
Water Soluble ◽  
Organic Solvent Extraction ◽  
Glycoside Linkage ◽  
Potential Applications ◽  
Tremendous Amount ◽  
Main Components ◽  
Hemicellulosic Sugars

AbstractAn efficient separation technology for hydrolysates towards a full valorization of bamboo is still a tough challenge, especially regarding the lignin and lignin-carbohydrate complexes (LCCs). The present study aimed to develop a facile approach using organic solvent extraction for efficiently fractionating the main components of bamboo hydrolysates. The high-purity lignin with only a trace of carbohydrates was first obtained by precipitation of the bamboo hydrolysate. The water-soluble lignin (WSL) fraction was extracted in organic solvent through a three-stage organic solvent extraction process, and the hemicellulosic sugars with increased purity were also collected. Furthermore, a thorough characterization including various NMR techniques (31P, 13C, and 2D-HSQC), GPC, and GC-MS was conducted to the obtained lignin-rich-fractions. It was found that the WSL fraction contained abundant functional groups and tremendous amount of LCC structures. As compared to native LCC of bamboo, the WSL fraction exhibited more typical LCC linkages, i.e. phenyl glycoside linkage, which is the main type of chemical linkage between lignin and carbohydrate in both LCC samples. The results demonstrate that organic phase extraction is a highly efficient protocol for the fractionation of hydrolysate and the isolation of LCC-rich streams possessing great potential applications.

scholarly journals Click Chemistry Enabling Covalent and Non-Covalent Modifications of Graphene with (Poly)saccharides

Polymers ◽  
2020 ◽  
Vol 13 (1) ◽  
pp. 142
Author(s):  
Hu Li ◽  
Raffaello Papadakis
Keyword(s):  
Click Chemistry ◽  
Life Science ◽  
Environmental Applications ◽  
Energy Materials ◽  
Sensors And Actuators ◽  
Polar Solvents ◽  
Wide Range ◽  
Potential Applications ◽  
Covalent Modifications

Graphene is a material with outstanding properties and numerous potential applications in a wide range of research and technology areas, spanning from electronics, energy materials, sensors, and actuators to life-science and many more. However, the insolubility and poor dispersibility of graphene are two major problems hampering its use in certain applications. Tethering mono-, di-, or even poly-saccharides on graphene through click-chemistry is gaining more and more attention as a key modification approach leading to new graphene-based materials (GBM) with improved hydrophilicity and substantial dispersibility in polar solvents, e.g., water. The attachment of (poly)saccharides on graphene further renders the final GBMs biocompatible and could open new routes to novel biomedical and environmental applications. In this review, recent modifications of graphene and other carbon rich materials (CRMs) through click chemistry are reviewed.

Electrochemical biosensor for detection of pathogenic bacteria based on dual signal amplification of Cu3(PO4)2-mediated click chemistry and DNAzyme

The Analyst ◽  
2021 ◽  
Author(s):  
Hongguo Wei ◽  
Jiayu Wan ◽  
Shengjun Bu ◽  
Wenguang Zhang ◽  
Ma Li ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Magnetic Separation ◽  
Concanavalin A ◽  
Signal Amplification ◽  
Pathogenic Bacteria ◽  
Electrochemical Biosensor ◽  
Inorganic Hybrid ◽  
Highly Sensitive ◽  
Antibody Conjugates ◽  
Dual Signal Amplification

A novel electrochemical biosensor for detecting pathogenic bacteria was designed based on specific magnetic separation and highly sensitive click chemistry. Instead of enzyme-antibody conjugates, organic-inorganic hybrid nanoflowers (Concanavalin A (Con...

scholarly journals Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts

1994 ◽  
Vol 304 (1) ◽  
pp. 263-269 ◽  
Author(s):  
R V Ward ◽  
S J Atkinson ◽  
J J Reynolds ◽  
G Murphy
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Plasma Membranes ◽  
Scatchard Analysis ◽  
Gelatinase A ◽  
Surface Binding ◽  
Binding Studies ◽  
Cell Surface Binding ◽  
Terminal Domain ◽  
Primary Fibroblasts

We report that the isolated C-terminal domain of progelatinase A is inhibitory to the activation of this proenzyme by primary skin fibroblast plasma membranes but is unable to inhibit organomercurial-induced self-cleavage and activation. Ligand binding studies demonstrate that fibroblasts stimulated with concanavalin A to activate progelatinase A have a significantly enhanced level of cell surface-associated progelatinase A. Tissue inhibitor of metalloproteinases-2 (TIMP-2), an effective inhibitor of membrane-mediated progelatinase A activation, is able to abolish the enhanced level of cell surface-associated progelatinase A that occurs following stimulation. TIMP-1, a poor inhibitor of membrane activation, is unable to inhibit the cell surface binding of progelatinase A. The enhancement in the binding of 125I-progelatinase A to fibroblasts following concanavalin A stimulation can be blocked by the inclusion of excess C-terminal gelatinase A but not by a truncated form of gelatinase A lacking the C-terminal domain. Scatchard analysis of the binding of 125I-progelatinase A to concanavalin A-stimulated fibroblasts has identified 950,000 gelatinase binding sites per cell with a Kd of 1.3 x 10(-8) M. Analysis of non-stimulated fibroblasts has identified 500,000 sites per cell with a Kd of 2.6 x 10(-8) M. We propose that membrane-mediated activation of progelatinase A involves binding of the proenzyme through its C-terminal domain to the cell surface and that TIMP-2 can inhibit activation by interaction with progelatinase A through the C-terminal domain, thus preventing binding of the proenzyme.

Glycosylation of polyphosphazenes by thiol-yne click chemistry for lectin recognition

RSC Advances ◽  
2015 ◽  
Vol 5 (21) ◽  
pp. 15909-15915 ◽  
Author(s):  
Chen Chen ◽  
Huang Xu ◽  
Yue-Cheng Qian ◽  
Xiao-Jun Huang
Keyword(s):  
Click Chemistry ◽  
Lectin Binding ◽  
Biological Systems ◽  
Binding Interactions ◽  
Lectin Recognition

Strong carbohydrate–lectin binding interactions in biological systems can be mimicked through the synthesis of glucose containing macromolecules, particularly glycosylated polymers.

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