Oligo-dendrimer inhibition of cholera toxin binding to GM1

J. P. Thompson, Cara-Lynne Schengrund

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

While GM1 is the cell surface receptor for cholera toxin, the free oligosaccharide portion of GM1 is not as effective a Hgand as clusters of the oligosaccharide are (Schengnmd & Ringlet, J. Biol. Chem. 264: 13233, 1989). Since gangliosides may exist in clusters in cell membranes (Hakomori, Biochem. Soc. Trans. 21: 583, 1993) and are known to form micelles in water, molecules with clustered GM1 oligosaccharide residues were synthesized as potential inhibitors. Dendrimers were used as the backbone for preparation of "polyvalent" oligosaccharides. First and second generation polyfpropylene iraine) dendrimers (de-Brabander-van den Berg and Meyer, Angew. Chem. Int. Ed. 32: 1308, 1993) were synthesized and the phenylisothiocyanate derivative of oligo-GMl coupled to each terminal primary amine. First generation dendrimers had 4 oligo-GMl residues, second, 8. Their effectiveness as inhibitors was determined by their ability to inhibit binding of 125I-labeled cholera toxin B subunit to GM1 coated microtiter wells. OligoGMl dendrimers inhibited binding of cholera toxin to the wells at concentrations -7.5 fold (4-mer) and -15 fold (8-mer) leas than native GM1.

Original languageEnglish (US)
JournalFASEB Journal
Volume10
Issue number6
StatePublished - Dec 1 1996

Fingerprint

Dendrimers
Cholera Toxin
Oligosaccharides
Gangliosides
Cell Surface Receptors
Micelles
Cell membranes
Amines
Cell Membrane
Derivatives
Molecules
Water
G(M1)-oligosaccharide

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Thompson, J. P., & Schengrund, C-L. (1996). Oligo-dendrimer inhibition of cholera toxin binding to GM1. FASEB Journal, 10(6).
Thompson, J. P. ; Schengrund, Cara-Lynne. / Oligo-dendrimer inhibition of cholera toxin binding to GM1. In: FASEB Journal. 1996 ; Vol. 10, No. 6.
@article{65c8f012163d457ab3f0ffbae2dc9764,
title = "Oligo-dendrimer inhibition of cholera toxin binding to GM1",
abstract = "While GM1 is the cell surface receptor for cholera toxin, the free oligosaccharide portion of GM1 is not as effective a Hgand as clusters of the oligosaccharide are (Schengnmd & Ringlet, J. Biol. Chem. 264: 13233, 1989). Since gangliosides may exist in clusters in cell membranes (Hakomori, Biochem. Soc. Trans. 21: 583, 1993) and are known to form micelles in water, molecules with clustered GM1 oligosaccharide residues were synthesized as potential inhibitors. Dendrimers were used as the backbone for preparation of {"}polyvalent{"} oligosaccharides. First and second generation polyfpropylene iraine) dendrimers (de-Brabander-van den Berg and Meyer, Angew. Chem. Int. Ed. 32: 1308, 1993) were synthesized and the phenylisothiocyanate derivative of oligo-GMl coupled to each terminal primary amine. First generation dendrimers had 4 oligo-GMl residues, second, 8. Their effectiveness as inhibitors was determined by their ability to inhibit binding of 125I-labeled cholera toxin B subunit to GM1 coated microtiter wells. OligoGMl dendrimers inhibited binding of cholera toxin to the wells at concentrations -7.5 fold (4-mer) and -15 fold (8-mer) leas than native GM1.",
author = "Thompson, {J. P.} and Cara-Lynne Schengrund",
year = "1996",
month = "12",
day = "1",
language = "English (US)",
volume = "10",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "6",

}

Thompson, JP & Schengrund, C-L 1996, 'Oligo-dendrimer inhibition of cholera toxin binding to GM1', FASEB Journal, vol. 10, no. 6.

Oligo-dendrimer inhibition of cholera toxin binding to GM1. / Thompson, J. P.; Schengrund, Cara-Lynne.

In: FASEB Journal, Vol. 10, No. 6, 01.12.1996.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Oligo-dendrimer inhibition of cholera toxin binding to GM1

AU - Thompson, J. P.

AU - Schengrund, Cara-Lynne

PY - 1996/12/1

Y1 - 1996/12/1

N2 - While GM1 is the cell surface receptor for cholera toxin, the free oligosaccharide portion of GM1 is not as effective a Hgand as clusters of the oligosaccharide are (Schengnmd & Ringlet, J. Biol. Chem. 264: 13233, 1989). Since gangliosides may exist in clusters in cell membranes (Hakomori, Biochem. Soc. Trans. 21: 583, 1993) and are known to form micelles in water, molecules with clustered GM1 oligosaccharide residues were synthesized as potential inhibitors. Dendrimers were used as the backbone for preparation of "polyvalent" oligosaccharides. First and second generation polyfpropylene iraine) dendrimers (de-Brabander-van den Berg and Meyer, Angew. Chem. Int. Ed. 32: 1308, 1993) were synthesized and the phenylisothiocyanate derivative of oligo-GMl coupled to each terminal primary amine. First generation dendrimers had 4 oligo-GMl residues, second, 8. Their effectiveness as inhibitors was determined by their ability to inhibit binding of 125I-labeled cholera toxin B subunit to GM1 coated microtiter wells. OligoGMl dendrimers inhibited binding of cholera toxin to the wells at concentrations -7.5 fold (4-mer) and -15 fold (8-mer) leas than native GM1.

AB - While GM1 is the cell surface receptor for cholera toxin, the free oligosaccharide portion of GM1 is not as effective a Hgand as clusters of the oligosaccharide are (Schengnmd & Ringlet, J. Biol. Chem. 264: 13233, 1989). Since gangliosides may exist in clusters in cell membranes (Hakomori, Biochem. Soc. Trans. 21: 583, 1993) and are known to form micelles in water, molecules with clustered GM1 oligosaccharide residues were synthesized as potential inhibitors. Dendrimers were used as the backbone for preparation of "polyvalent" oligosaccharides. First and second generation polyfpropylene iraine) dendrimers (de-Brabander-van den Berg and Meyer, Angew. Chem. Int. Ed. 32: 1308, 1993) were synthesized and the phenylisothiocyanate derivative of oligo-GMl coupled to each terminal primary amine. First generation dendrimers had 4 oligo-GMl residues, second, 8. Their effectiveness as inhibitors was determined by their ability to inhibit binding of 125I-labeled cholera toxin B subunit to GM1 coated microtiter wells. OligoGMl dendrimers inhibited binding of cholera toxin to the wells at concentrations -7.5 fold (4-mer) and -15 fold (8-mer) leas than native GM1.

UR - http://www.scopus.com/inward/record.url?scp=33749116027&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749116027&partnerID=8YFLogxK

M3 - Article

VL - 10

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 6

ER -

Thompson JP, Schengrund C-L. Oligo-dendrimer inhibition of cholera toxin binding to GM1. FASEB Journal. 1996 Dec 1;10(6).