Abstract
Carbohydrates, which are defined as polyhydroxyaldehydes or polyhydroxyketones, or larger compounds that can be hydrolyzed into such units, are ubiquitous in the living world. Carbohydrates act as the sources of energy and carbon in plants and animals and are the important structural elements in plant cell walls as well as in the extracellular matrix of animal and human tissues. Like nucleic acids and proteins, carbohydrates are involved in many biological processes and metabolism and seem to play critical roles in determining biological functions [1]. Glycosylation also affects the biological activity, lifetime, cellular uptake, and specificity of these proteins [2]. Therefore, the study and characterization of carbohydrates has become increasingly important and has emerged as the “new frontier” for elucidating fundamental biochemical processes and for identifying new pharmaceutical substances.
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References
Jelinek, R., Kolusheva, S.: Carbohydrate biosensors. Chem. Rev. 104, 5987–6016 (2004)
Mikkers, F.E.P., Everaerts, F.M., Verheggen, T.P.E.M.: High-performance zone electrophoresis. J. Chromatogr. A 169, 11–20 (1979)
Wang, J.: Electrochemical glucose biosensors. Chem. Rev. 108, 814–825 (2007)
Newman, J.D., Turner, A.P.F.: Home blood glucose biosensors: a commercial perspective. Biosens. Bioelectron. 20, 2435–2453 (2005)
Varki, A., Manzi, A.E., Freeze, H.H.: Introduction: preparation and analysis of glycoconjugates. In: Ausubel, F.M. (ed.) Current Protocols in Molecular Biology, Unit 17.0. Wiley, New York (1996)
Lis, H., Sharon, N.: Protein glycosylation – structural and functional aspects. Eur. J. Biochem. 218, 1–27 (1993)
Laine, R.A.: A calculation of all possible oligosaccharide isomers both branched and linear yields 1.05 × 1012 structures for a reducing hexasaccharide: the isomer barrier to development of single-method saccharide sequencing or synthesis systems. Glycobiology 4, 759–767 (1994)
Varki, A.: Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97–130 (1993)
Furukawa, K., Kobata, A.: Protein glycosylation. Curr. Opin. Biotechnol. 3, 554–559 (1992)
Hascall, V.C., Calabro, A., Midura, R.J., et al.: Isolation and characterization of proteoglycans. Meth. Enzymol. 230, 390–417 (1994)
Hart, G.W.: Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 66, 315–335 (1997)
Varki, A., Marth, J.: Oligosaccharides in vertebrate development. Semin. Dev. Biol. 6, 127–138 (1995)
Muramatsu, T.: Carbohydrate signals in metastasis and prognosis of human carcinomas. Glycobiology 3, 291–296 (1993)
Fukuda, M.: Possible roles of tumor-associated carbohydrate antigens. Cancer Res. 56, 2237–2244 (1996)
Kim, Y.J., Varki, A.: Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconj. J. 14, 569–576 (1997)
Galili, U., Shohet, S.B., Kobrin, E., et al.: Man, apes and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells. J. Biol. Chem. 263, 17755–17762 (1988)
Manzella, S.M., Dharmesh, S.M., Beranek, M.C., et al.: Evolutionary conservation of the sulfated oligosaccharides on vertebrate glycoprotein hormones that control circulatory half-life. J. Biol. Chem. 270, 21665–21671 (1995)
Hart, G.W.: Glycosylation. Curr. Opin. Cell Biol. 4, 1017–1023 (1992)
Paulson, J.C.: Glycoproteins: what are the sugar chains for? Trends Biochem. Sci. 14, 272–276 (1989)
Drickamer, K., Taylor, M.E.: Evolving views of protein glycosylation. Trends Biochem. Sci. 23, 321–324 (1998)
Gahmberg, C.G., Tolvanen, M.: Why mammalian cell surface proteins are glycoproteins. Trends Biochem. Sci. 21, 308–311 (1996)
Crocker, P.R., Feizi, T.: Carbohydrate recognition systems: functional triads in cell–cell interactions. Curr. Opin. Struct. Biol. 6, 679–691 (1996)
Nelson, R.M., Venot, A., Bevilacqua, M.P., et al.: Carbohydrate–protein interactions in vascular biology. Ann. Rev. Cell. Dev. Biol. 11, 601–631 (1995)
Cummings, R.D.: Use of lectins in analysis of glycoconjugates. Meth. Enzymol. 230, 66–86 (1994)
Gagneux, P., Varki, A.: Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9, 747–755 (1999)
Fischer, E.: Influence of the configuration on the activity of the enzyme. Ber. Chem. Ges. 27, 2985–2993 (1894)
Phillips, D.C.: The three-dimensional structure of an enzyme molecule. Sci. Am. 215, 78–90 (1996)
Blake, C.C., Johnson, L.N., Mair, G.A., et al.: Crystallographic studies of the activity of hen egg-white lysozyme. Proc. R. Soc. Lond. B Biol. Sci. 167, 378–388 (1967)
Rini, J.M.: Lectin structure. Ann. Rev. Biophys. Biomol. Struct. 24, 551–577 (1995)
Quiocho, F.A.: Carbohydrate-binding proteins: tertiary structures and protein–sugar interactions. Annu. Rev. Biochem. 55, 287–315 (1986)
Wilson, K.A., Skehel, J.J., Wiley, D.C.: Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3-Á resolution. Nature 289, 366–373 (1981)
Hardman, K.D., Ainsworth, C.F.: Structure of concanavalin A at 2.4-Ǻ resolution. Biochemistry 11, 4910–4919 (1972)
Edelman, G.M., Gunningham, B.A., Reeke Jr., G.N., et al.: The covalent and three-dimensional structure of concanavalin A. Proc. Natl. Acad. Sci. 69, 2580–2584 (1972)
Kabat, E.A., Liao, J., Lemieux, R.U.: Immunochemical studies on blood groups-LXVIII. The combining site of anti-I Ma (group 1). Immunochemistry 15, 727–731 (1978)
Baldwin, R.P.: Electrochemical determination of carbohydrates: enzyme electrodes and amperometric detection in liquid chromatography and capillary electrophoresis. J. Pharm. Biomed. Anal. 19, 69–81 (1999)
Whitham, K.M., Hadley, J.L., Morris, H.G., et al.: Analytical applications of carbon nanotubes: a review. Glycobiology 9, 285–291 (1999)
He, L., Sato, K., Abo, M., et al.: Separation of saccharides derivatized with 2-aminobenzoic acid by capillary electrophoresis and their structural consideration by nuclear magnetic resonance. Anal. Biochem. 314, 128–134 (2003)
Gao, S., Wang, W., Wang, B.: Building fluorescent sensors for carbohydrates using template-directed polymerizations. Bioorg. Chem. 29, 308–320 (2001)
Akimitsu, K., Hidenobu, Y., Toshifumi, T.: Sialic acid imprinted polymer-coated quartz crystal microbalance. Electroanalysis 12, 1322–1326 (2000)
van Kerkhof, J.C., Bergveld, P., Schasfoort, R.B.M.: The ISFET based heparin sensor with a monolayer of protamine as affinity ligand. Biosens. Bioelectron. 10, 269–282 (1995)
Bush, C.A., Martin-Pastor, M., Imbery, A.: Structure and conformation of complex carbohydrates of glycoproteins, glycolipids, and bacterial polysaccharides. Annu. Rev. Biophys. Biomol. Struct. 28, 269–293 (1999)
McReynolds, K.D., Gervay-Hague, J.: Examining the secondary structures of unnatural peptides and carbohydrate-based compounds utilizing circular dichroism. Tetrahedron Asymmetr. 11, 337–362 (2000)
D’Auria, S., DiCesare, N., Staiano, M., et al.: A novel fluorescence competitive assay for glucose determinations by using a thermostable glucokinase from the thermophilic microorganism Bacillus stearothermophilus. Anal. Biochem. 303, 138–144 (2002)
Lerouxel, O., Choo, T.S., Seveno, M., et al.: Rapid structural phenotyping of plant cell wall mutants by enzymatic oligosaccharide fingerprinting. Plant Physiol. 130, 1754–1763 (2002)
Thanawiroon, C., Rice, K.G., Toida, T., et al.: Liquid chromatography/mass spectrometry sequencing approach for highly sulfated heparin-derived oligosaccharides. J. Biol. Chem. 279, 2608–2615 (2004)
Paulus, A., Klockow, A.: Detection of carbohydrates in capillary electrophoresis. J. Chromatogr. A 720, 353–376 (1996)
Starr, C.M., Irene Masada, R., Hague, C., et al.: Fluorophore-assisted carbohydrate electrophoresis in the separation, analysis, and sequencing of carbohydrates. J. Chromatogr. A 720, 295–321 (1996)
Shigeo, S., Susumu, H.: A tabulated review of capillary electrophoresis of carbohydrates. Electrophoresis 19, 2539–2560 (1998)
Penn, S.G., He, L., Natan, M.J.: Nanoparticles for bioanalysis. Curr. Opin. Chem. Biol. 7, 609–615 (2003)
Wang, J.: Nanomaterial-based amplified transduction of biomolecular interactions. Small 1, 1036–1043 (2005)
Christof, M.N.: Nanoparticles, proteins, and nucleic acids: biotechnology meets materials science. Angew. Chem. Int. Ed. 40, 4128–4158 (2001)
Eugenii, K., Itamar, W.: Integrated nanoparticle-biomolecule hybrid systems: synthesis, properties, and applications. Angew. Chem. Int. Ed. 43, 6042–6108 (2004)
Alivisatos, P.: The use of nanocrystals in biological detection. Nat. Biotechnol. 22, 47–52 (2004)
Punit, K., Marc, W., Charles, R.M.: Nanotube membrane based biosensors. Electroanalysis 16, 9–18 (2004)
Rosi, N.L., Mirkin, C.A.: Nanostructures in biodiagnostics. Chem. Rev. 105, 1547–1562 (2005)
Wang, J.: Carbon-nanotube based electrochemical biosensors: a review. Electroanalysis 17, 7–14 (2005)
Gooding, J.J.: Nanostructuring electrodes with carbon nanotubes: a review on electrochemistry and applications for sensing. Electrochim. Acta 50, 3049–3060 (2005)
Trojanowicz, M.: Analytical applications of carbon nanotubes: a review. Trac Trends Anal. Chem. 25, 480–489 (2006)
Allen, B.L., Kichambare, P.D., Star, A.: Carbon nanotube field-effect-transistor-based biosensors. Adv. Mater. 19, 1439–1451 (2007)
Javey, A., Wang, Q., Ural, A., et al.: Carbon nanotube transistor arrays for multistage complementary logic and ring oscillators. Nano Lett. 2, 929–932 (2002)
Javey, A., Tu, R., Farmer, D.B., et al.: High performance n-type carbon nanotube field-effect transistors with chemically doped contacts. Nano Lett. 5, 345–348 (2005)
Wang, J.: Portable electrochemical systems. Trac Trends Anal. Chem. 21, 226–232 (2002)
Wang, J.: Electrochemical detection for microscale analytical systems: a review. Talanta 56, 223–231 (2002)
Kerman, K., Saito, M., Tamiya, E., et al.: Nanomaterial-based electrochemical biosensors for medical applications. Trac Trends Anal. Chem. 27, 585–592 (2008)
Jorgenson, J.W., Lukacs, K.D.: Zone electrophoresis in open tubular glass capillaries. Anal. Chem. 53, 1298–1302 (1981)
Sims, M.J., Li, Q., Kachoosangi, R.T., et al.: Using multiwalled carbon nanotube modified electrodes for the adsorptive striping voltammetric determination of hesperidin. Electrochim. Acta 54, 5030–5034 (2009)
Prabhu, S.V., Baldwin, R.P.: Constant potential amperometric detection of carbohydrates at a copper-based chemically modified electrode. Anal. Chem. 61, 852–856 (1989)
Luo, P., Prabhu, S.V., Baldwin, R.P.: Constant potential amperometric detection at a copper-eased electrode: electrode formation and operation. Anal. Chem. 62, 752–755 (1990)
Reim, R.E., Van Effen, R.M.: Determination of carbohydrates by liquid chromatography with oxidation at a nickel(III) oxide electrode. Anal. Chem. 58, 3203–3207 (1986)
Cataldi, T.R.I., Casella, I.G., Desimoni, E., et al.: Cobalt-based glassy carbon chemically modified electrode for constant-potential amperometric detection of carbohydrates in flow-injection analysis and liquid chromatography. Anal. Chim. Acta 270, 161–171 (1992)
Wang, J., Taha, Z.: Catalytic oxidation and flow detection of carbohydrates at ruthenium dioxide modified electrodes. Anal. Chem. 62, 1413–1416 (1990)
Elahi, M.Y., Mousavi, M.F., Ghasemi, S.: Nano-structured Ni(II)-curcumin modified glassy carbon electrode for electrocatalytic oxidation of fructose. Electrochim. Acta 54, 490–498 (2008)
You, T., Niwa, O., Chen, Z., et al.: An amperometric detector formed of highly dispersed Ni nanoparticles embedded in a graphite-like carbon film electrode for sugar determination. Anal. Chem. 75, 5191–5196 (2003)
Sharon, N.: Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chem. Rev. 98, 637–674 (1998)
Dai, Z., Kawde, A.N., Xiang, Y., et al.: Nanoparticle-based sensing of glycan lectin interactions. J. Am. Chem. Soc. 128, 10018–10019 (2006)
Ding, L., Ji, Q.J., Qian, R.C., et al.: Lectin-based nanoprobes functionalized with enzyme for highly sensitive electrochemical monitoring of dynamic carbohydrate expression on living cells. Anal. Chem. 82, 1292–1298 (2010)
Earhart, C., Jana, N.R., Erathodiyil, N., et al.: Synthesis of carbohydrate-conjugated nanoparticles and quantum dots. Langmuir 24, 6215–6219 (2008)
Babu, P., Sinha, S., Surolia, A.: Sugar quantum dot conjugates for a selective and sensitive detection of lectins. Bioconjug. Chem. 18, 146–151 (2006)
Nagaraj, V.J., Eaton, S., Thirstrup, D., et al.: Piezoelectric printing and probing of lectin NanoProbeArrays for glycosylation analysis. Biochem. Biophys. Res. Commun. 375, 526–530 (2008)
Zheng, T., Peelen, D., Smith, L.M.: Lectin arrays for profiling cell surface carbohydrate expression. J. Am. Chem. Soc. 127, 9982–9983 (2005)
Noriko, N., Shin-Ichiro, N.: Direct and efficient monitoring of glycosyltransferase reactions on gold colloidal nanoparticles by using mass spectrometry. Chem. Eur. J. 12, 6478–6485 (2006)
Sato, Y., Murakami, T., Yoshioka, K., et al.: 12-Mercaptododecyl β-maltoside-modified gold nanoparticles: specific ligands for concanavalin A having long flexible hydrocarbon chains. Anal. Bioanal. Chem. 391, 2527–2532 (2008)
Honda, S., Iwase, S., Makino, A., et al.: Simultaneous determination of reducing monosaccharides by capillary zone electrophoresis as the borate complexes of N-2-pyridylglycamines. Anal. Biochem. 176, 72–77 (1989)
Gao, J., Liu, D., Wang, Z.: Microarray-based study of carbohydrate protein-binding by gold nanoparticle probes. Anal. Chem. 80, 8822–8827 (2008)
Lin, C.C., Yeh, Y.C., Yang, C.Y., et al.: Quantitative analysis of multivalent interactions of carbohydrate-encapsulated gold nanoparticles with concanavalin A. Chem. Commun. 23, 2920–2921 (2003)
Guo, C., Boullanger, P., Jiang, L., et al.: Highly sensitive gold nanoparticles biosensor chips modified with a self-assembled bilayer for detection of Con A. Biosens. Bioelectron. 22, 1830–1834 (2007)
Lin, C.C., Yeh, Y.C., Yang, C.Y., et al.: Selective binding of mannose-encapsulated gold nanoparticles to type 1 pili in Escherichia coli. J. Am. Chem. Soc. 124, 3508–3509 (2002)
Niikura, K., Nagakawa, K., Ohtake, N., et al.: Gold nanoparticle arrangement on viral particles through carbohydrate recognition: a non-cross-linking approach to optical virus detection. Bioconjug. Chem. 20, 1848–1852 (2009)
Gu, L.R., Luo, P.J.G., Wang, H.F., et al.: Single-walled carbon nanotube as a unique scaffold for the multivalent display of sugars. Biomacromolecules 9, 2408–2418 (2008)
Chikae, M., Fukuda, T., Kerman, K., et al.: Amyloid-β detection with saccharide immobilized gold nanoparticle on carbon electrode. Bioelectrochemistry 74, 118–123 (2008)
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Ju, H., Zhang, X., Wang, J. (2011). Carbohydrate Detection Using Nanostructured Biosensing. In: NanoBiosensing. Biological and Medical Physics, Biomedical Engineering. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-9622-0_14
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