Solid-phase chemical tools for glycobiology - Oligonucleotides

Solid-phase chemical tools for glycobiology
Received 17 February 2006; revised 25 April 2006; accepted 28 April 2006. Available online 22 May 2006.
Kim Larsena, Mikkel B. Thygesena, Fanny Guillaumieb, William G.T. Willatsc and Knud J. Jensena, ,
Carbohydrate Research
Volume 341, Issue 10 , 24 July 2006
ScienceDirect
aDepartment of Natural Sciences, Section for Bioorganic Chemistry, Royal Veterinary and Agricultural University, DK-1871 Frederiksberg, Denmark
bNovozymes Biopolymer A/S, DK-2880 Bagsvaerd, Denmark
cDepartment of Plant Physiology, Institute of Molecular Biology and Physiology, The University of Copenhagen, DK-1353 Copenhagen, Denmark
Abstract
Techniques involving solid supports have played crucial roles in the development of genomics, proteomics, and in molecular biology in general. Simularly, methods for immobilization or attachment to surfaces and resins have become ubiquitous in sequencing, synthesis, analysis, and screening of oligonucleotides, peptides, and proteins. However, solid-phase tools have been employed to a much lesser extent in glycobiology and glycomics. This review provides a comprehensive overview of solid-phase chemical tools for glycobiology including methodologies and applications. We provide a broad perspective of different approaches, including some well-established ones, such as immobilization in microtiter plates and to cross-linked polymers. Emerging areas such as glycan microarrays and glycan sequencing, quantum dots, and gold nanoparticles for nanobioscience applications are also discussed. The applications reviewed here include enzymology, immunology, elucidation of biosynthesis, and systems biology, as well as first steps toward solid-supported sequencing. From these methods and applications emerge a general vision for the use of solid-phase chemical tools in glycobiology.
Keywords: Microarrays; Nanoparticles; Quantum dots; PEGA; Nanobioscience; Glycomics; Microtiter plates; ELISA; ELLA
Abbreviations: a3GalT, a-(1?3)-galactosyltransferase; ADL, Arundo donax lectin; Aoa, amino-oxyacetyl; CD, cyclodextrin; CEL, Cucumaria echinata lectin; CF, cystic fibrosis; Con A, concanavalin A; DIOS, desorption/ionization on silicon; DTT, dithiotreitol; EDC, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide; ELISA, enzyme-linked immunosorbent assay; ELLA, enzyme-linked lectin assay; FGF, fibroblast growth factors; FimH, minor type 1 fimbrial subunit, membrane-specific adhesin; FITC, fluorescein isothiocyanate; GAG, glycosaminoglycans; Gal 6, galectin LEC-6; GalAT, a1,4-galacturonosyltransferase; GNP, glyconanoparticle; GnT-V, 5'-diphospho-N-acetylglucosamine:a-mannoside ?-(1?6)-N-acetylglucosaminyltransferase; gp120, HIV envelope glycoprotein; GPA, erythrocyte glycophorin; HEV32, hevein-derived peptide; HRP (HPR), horseradish peroxidase; LCA, Lens culinaris (lentil) lectin; NGL, neoglycolipid; NHS, N-hydroxysuccinimidyl; OGA, oligogalacturonates; PA, pyridylaminated; PAA, polyacrylamide; PA-IL, Pseudomonas aeruginosa agglutinin; PEGA, polyethylene glycol dimethylacrylamide copolymer; PHA, Phaseolus vulgaris (red kidney bean); PNGase F, peptide N-glycosidase F; PRV gC, Pseudorabies virus glycoprotein C; QD, quantum dots; RANTES, regulated on activation, normal T-cell expressed, and secreted; RCA, Ricinus communis agglutinin; SBE, starch branching enzyme; SNA, Sambucus nigra agglutinin; SP-D, surfactant protein D; SPE, solid-phase extraction; SPR, surface plasmon resonance; TBS, Tris-buffer saline; TF, Thomsen?Friedenreich; TFA, trifluoroacetic acid; TOPO, trioctylphosphine oxide; VAA, Viscum album agglutinin; WGA, wheat germ agglutinin

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