Neoglycoconjugates

Lee, Reiko T.; Lee, Yuan C.

doi:10.1002/9783527614738.ch4

Cited by 6 publications

(5 citation statements)

References 95 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The number of bound probe molecules at saturation ( B max ; Table 1) indicated that at least 10% of the perlucin molecules had been immobilized in a functional state. However, this should be taken as lower limit because binding was reduced by 50% with a threefold reduction in the sugar content of the neoglycoprotein indicating that cluster effects, with the carbohydrates on one probe molecule making contact to several CRDs [32], also played a role.…”

Section: Resultsmentioning

confidence: 99%

The amino‐acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin

Mann¹,

Weiss²,

André³

et al. 2000

European Journal of Biochemistry

150

View full text Add to dashboard Cite

Perlucin isolated from abalone nacre consists of 155 amino acids including a glycosylated asparagine. The sequence of the first 130 amino acids shows a high similarity to the C-type carbohydrate-recognition domains of asialoglycoprotein receptors and other members of the group of C-type lectins but also a weaker similarity to related proteins without carbohydrate-binding activity. This C-type module is followed by a short C-terminal domain containing two almost identical sequence repeats with a length of 10 amino acids. Solid phase assays show a divalent metal ion-dependent binding of perlucin to (neo)glycoproteins containing d-galactose or d-mannose/d-glucose indicating that perlucin is a functional C-type lectin with broad carbohydrate-binding specificity. Our results also indicate that it may be difficult to predict carbohydrate-binding specificity and the occurrence of alternative binding configurations by amino-acid sequence comparisons and homology modeling.

show abstract

Section: Resultsmentioning

confidence: 99%

The amino‐acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin

Mann¹,

Weiss²,

André³

et al. 2000

European Journal of Biochemistry

150

View full text Add to dashboard Cite

show abstract

“…Neoglycoproteins can be also prepared from bioactive proteins such as enzymes, immunoglobulins, or growth factors. A variety of strategies have been employed in preparing neoglycoproteins (neoglycoenzymes) using mono-, oligo-, or polysaccharides (Magnusson et al, 1994;Lee and Lee, 1997).…”

Section: Introductionmentioning

confidence: 99%

Neoglycoconjugates of Mannan with Bovine Serum Albumin and Their Interaction with Lectin Concanavalin A

et al. 2001

View full text Add to dashboard Cite

Neoglycoconjugates were prepared from mannan isolated from yeast Saccharomyces cerevisiae and activated by periodate oxidation to create aldehyde groups. Various degrees of oxidation introduced 11-28 aldehyde groups per mannan molecule and simultaneously resulted in a molar mass decrease from 46 to 44.5-31 kDa. The activated mannans were subsequently conjugated with bovine serum albumin forming neoglycoconjugates. Some parameters of these mannan-bovine serum albumin conjugates were characterized: saccharide content 25-30% w/w, molar mass within the range 169-246 kDa, and polydispersion (M(w)/M(n)) from 2.8 to 3.6. The interaction of these conjugates with lectin concanavalin A was studied using three different methods: (i) quantitative precipitation in solution; (ii) sorption to concanavalin A immobilized on bead cellulose; and (iii) kinetic measurement of the interaction by surface plasmon resonance. Quantitative precipitation assay showed only negligible differences in the precipitation course of original mannan and the corresponding mannan-bovine serum albumin conjugates. Both the sorption method (equilibrium method) and the surface plasmon resonance measurement (kinetic method) demonstrates that the values of dissociation constant K(D) of all synthetic neoglycoconjugates were within the range 10(-7) - 10(-8) mol x L(-1) (close to K(D) = 10(-8) mol x L(-1) determined by the sorption method for the original mannan). In conclusion, characterization of synthetic neoglycoconjugates confirmed that the method used for their preparation retained the ability of mannan moiety to interact with concanavalin A.

show abstract

“…Physiologically, the recognition of distinct carbohydrate ligands by lectins is involved in various functionally important processes such as cell adhesion or glycoprotein routing (). This wide-ranging relevance of protein−carbohydrate interactions explains the efforts to construct tailor-made neoglycoconjugates as defined tools to explore medical applications ( , ). Already experimentally verified possibilities encompass lectin-mediated drug targeting, especially to the C-type asialoglycoprotein receptor of hepatocytes, and lectin visualization in morphological or diagnostic approaches ( − ).…”

Section: Introductionmentioning

confidence: 99%

Neoglycoproteins with the Synthetic Complex Biantennary Nonasaccharide or Its α2,3/α2,6-Sialylated Derivatives: Their Preparation, Assessment of Their Ligand Properties for Purified Lectins, for Tumor Cells in Vitro, and in Tissue Sections, and Their Biodistribution in Tumor-Bearing Mice

et al. 1997

View full text Add to dashboard Cite

Neoglycoproteins were prepared with chemoenzymatically synthesized complex biantennary N-glycan derivatives the nonreducing ends of which bear typical sequences found in glycoproteins. A chemically obtained biantennary heptasaccharide-azide was reduced and acylated with a 6-aminohexanoyl spacer. Elongation of the deprotected heptasaccharide using glycosyltransferases yielded a biantennary nonasaccharide with terminal galactose residues and two undecasaccharides terminating with alpha 2,6- or alpha 2,3-linked sialic acid. The free amino group of the spacer of these oligosaccharides was converted into an isothiocyanate. Its subsequent coupling to bovine serum albumin gave neoglycoproteins with a yield of 2.4-3.6 glycan chains per carrier molecule. This versatile synthetic pathway allows employment of a wide variety of complex-type glycans, which can be introduced to various test systems in vitro and in vivo to evaluate potential biomedical applications. Solid-phase assays with biotinylated sugar receptors revealed discriminatory binding properties of the three neoglycoproteins, especially for the mistletoe lectin. This direct assay system is preferable to the measurement of inhibitory capacities with respect to model ligands. Ligand type- and cell type-dependent quantitative differences in the binding properties of the probes were detected by FACScan analyses with a panel of tumor cell lines and by monitoring of staining in tissue sections for small cell and non-small-cell lung cancer and mesotheliomas. Biodistribution of iodinated neoglycoproteins in mice gave a prolonged presence of the sialylated probes in serum. Relative to the nonasaccharide, the uptake, especially of the iodinated neoglycoprotein with alpha 2,3-sialylated ligand chains, was clearly elevated in mice for kidneys and Ehrlich tumors. On the basis of the documented feasibility of these applications, it is concluded that the further elaboration of glycan chain variants by the described synthetic approach in combination with the given test panel is warranted to evaluate the potential of complex glycan chain-carrying neoglycoproteins for diagnostic and therapeutic purposes.

show abstract

Neoglycoconjugates

Cited by 6 publications

References 95 publications

The amino‐acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin

The amino‐acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin

Neoglycoconjugates of Mannan with Bovine Serum Albumin and Their Interaction with Lectin Concanavalin A

Neoglycoproteins with the Synthetic Complex Biantennary Nonasaccharide or Its α2,3/α2,6-Sialylated Derivatives: Their Preparation, Assessment of Their Ligand Properties for Purified Lectins, for Tumor Cells in Vitro, and in Tissue Sections, and Their Biodistribution in Tumor-Bearing Mice

Contact Info

Product

Resources

About