Lectins: tools for the molecular understanding of the glycocode

Ambrosi, Moira; Cameron, Neil R.; Davis, Benjamin G.

doi:10.1039/b414350g

Cited by 446 publications

(371 citation statements)

References 154 publications

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“…9- 13 The ability of some of these materials to specifically recognize lectins and cell surfaces has been the subject of extensive research, and now that the development of novel therapeutic strategies can be based on multivalent interactions a better understanding of these factors is required. [13][14][15][16] A number of different strategies have been employed for the synthesis of the required multivalent carbohydrate ligands.…”

Section: Introductionmentioning

confidence: 99%

“…3, [13][14][15] For ligand comparative studies it is therefore of importance to have a set of synthetic tools that allows for the synthesis of libraries of polymers having identical macromolecular features, with the relative density of epitope binding units being the only variable. Postpolymerization processes appear to be the only way for achieving this goal as long as extremely efficient grafting processes are available.…”

Section: Introductionmentioning

confidence: 99%

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Site-Directed Conjugation of “Clicked” Glycopolymers To Form Glycoprotein Mimics: Binding to Mammalian Lectin and Induction of Immunological Function

et al. 2007

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Synthesis of well-defined neoglycopolymer-protein biohybrid materials and a preliminary study focused on their ability of binding mammalian lectins and inducing immunological function is reported. Crucial intermediates for their preparation are well-defined maleimide-terminated neoglycopolymers (Mn ) 8-30 kDa; Mw/Mn ) 1.20-1.28) presenting multiple copies of mannose epitope units, obtained by combination of transition-metal-mediated living radical polymerization (TMM LRP) and Huisgen [2+3] cycloaddition. Bovine serum albumin (BSA) was employed as single thiol-containing model protein, and the resulting bioconjugates were purified following two independent protocols and characterized by circular dichroism (CD) spectroscopy, SDS PAGE, and SEC HPLC. The versatility of the synthetic strategy presented in this work was demonstrated by preparing a small library of conjugating glycopolymers that only differ from each other for their relative epitope density were prepared by coclicking of appropriate mixtures of mannopyranoside and galactopyranoside azides to the same polyalkyne scaffold intermediate. Surface plasmon resonance binding studies carried out using recombinant rat mannose-binding lectin (MBL) showed clear and dose-dependent MBL binding to glycopolymer-conjugated BSA. In addition, enzyme-linked immunosorbent assay (ELISA) revealed that the neoglycopolymer-protein materials described in this work possess significantly enhanced capacity to activate complement via the lectin pathway when compared with native unmodified BSA.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Site-Directed Conjugation of “Clicked” Glycopolymers To Form Glycoprotein Mimics: Binding to Mammalian Lectin and Induction of Immunological Function

et al. 2007

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“…An essential tool for the specific recognition of sugars has been the lectin class of carbohydrate-binding proteins (Cummings, 1994). Lectins interact with complex carbohydrates in a non-covalent manner that is usually both reversible and highly specific (Ambrosi et al, 2005;Naeem et al, 2007). That lectin-carbohydrate interactions can also be exploited in modern proteomic applications has been shown by numerous studies (Qiu and Regnier, 2005;Ohtsu et al, 2005;Durham and Regnier, 2006).…”

Section: Introductionmentioning

confidence: 99%

Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation

O’Connell

Doran

Gannon

et al. 2008

European Journal of Cell Biology

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Since various neuromuscular diseases are associated with abnormal glycosylation, it was of interest to determine whether this key post-translational modification is also altered in aged skeletal muscle. Lectins represent highly versatile carbohydrate-binding proteins that are routinely employed for the characterization of glycoproteins. Here, we used the lectin wheat germ agglutinin (WGA) for the proteomic profiling of senescent fibers. WGA labeling of the soluble proteome from 3-month-versus 30-month-old rat gastrocnemius muscle, following two-dimensional gel electrophoretic separation, resulted in the identification of 13 distinct protein species. Analysis of WGA binding levels, in conjunction with mass spectrometric fingerprinting, revealed that one isoform of a major metabolic muscle protein exhibited a drastic alteration in the content of sialic acid and N-acetylglucosaminyl sugar residues. Pyruvate kinase isoform M1 with protein accession number gi|16757994|, exhibiting a pI of 6.6 and an apparent molecular mass of 57.8 kDa, showed a six fold increase in N-glycosylation and a three fold decrease in protein expression. In contrast to comparable levels of N-glycosylated proteins in young adult versus senescent muscle, as judged by fluoresceinconjugated WGA labeling of transverse muscle cryosections, staining with antibodies to the M1 isoform of pyruvate kinase showed reduced expression of this cytosolic element. Furthermore, activity assays demonstrated a reduced activity of this glycolytic enzyme in senescent muscle. This agrees with the idea that abnormal post-translational modifications in key metabolic enzymes may be involved in the conversion of aged muscle to slower twitch patterns and a drastic shift to more aerobic-oxidative metabolism.

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“…59 These thermo-and pH-responsive glycopolymers showed lectin (Concanavalin A) binding which renders them useful for cell targeting in diagnostic or therapeutic applications. 78 Lectin binding microspheres have been fabricated based on the irreversible LCST behavior of PiPropOx. PiPropOx undergoes irreversible crystallization upon long-term annealing above 60 °C, resulting in the formation of coagulate particles.…”

Section: Applications Of Poly(2-oxazoline)s With Clickable Side Chainsmentioning

confidence: 99%

Poly(2-oxazoline)s and click chemistry: A versatile toolbox toward multi-functional polymers

Lava

Verbraeken

Hoogenboom

2015

European Polymer Journal

134

105

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Poly(2-alkyl/aryl-2-oxazoline)s (PAOx) have been gaining increasing attention because they combine biocompatibility with so-called stealth behavior, making them ideal candidates for use in a wide variety of biomedical applications. Especially, the possibility of side-chain modification makes them a valuable alternative to poly(ethylene glycol), currently the gold standard amongst biocompatible polymers. Nevertheless, the cationic ring opening polymerization of 2-oxazolines is not compatible with nucleophilic entities, for example hydroxyl and amine moieties. Therefore, the modular approach of 'click chemistry' offers an elegant strategy towards functional PAOx by postpolymerization modification of PAOx that contain clickable groups. This feature describes the synthesis of PAOx with such clickable entities at the chain-end or in the side-chain, as well as their potential (bio)materials applications.

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Lectins: tools for the molecular understanding of the glycocode

Cited by 446 publications

References 154 publications

Site-Directed Conjugation of “Clicked” Glycopolymers To Form Glycoprotein Mimics: Binding to Mammalian Lectin and Induction of Immunological Function

Site-Directed Conjugation of “Clicked” Glycopolymers To Form Glycoprotein Mimics: Binding to Mammalian Lectin and Induction of Immunological Function

Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation

Poly(2-oxazoline)s and click chemistry: A versatile toolbox toward multi-functional polymers

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