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Multivalent scaffolds induce galectin-3 aggregation into nanoparticles.

Candace K Goodman1, Mark L Wolfenden1, Pratima Nangia-Makker2

  • 1Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, USA.

Beilstein Journal of Organic Chemistry
|August 28, 2014
PubMed
Summary
This summary is machine-generated.

Lactose-functionalized dendrimers induce multivalent aggregation of galectin-3, a protein implicated in cancer. The size of these galectin-3-dendrimer aggregates is controllable by dendrimer generation, offering insights into sugar-binding protein function.

Keywords:
dendrimersgalectin-3glycodendrimersmultivalencymultivalent glycosylationprotein aggregation

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Cancer Biology

Background:

  • Galectin-3 mediates cell surface glycoprotein clustering and lattice formation.
  • Galectin-3 is implicated in cancer progression, including tumor embolization and survival.

Purpose of the Study:

  • To investigate the interaction between lactose-functionalized dendrimers and galectin-3.
  • To characterize the resulting aggregates and understand the regulation of galectin-3 aggregation.

Main Methods:

  • Dynamic light scattering
  • Fluorescence microscopy
  • Characterization of glycodendrimer-galectin aggregates

Main Results:

  • Lactose-functionalized dendrimers interact with galectin-3 in a multivalent manner, forming aggregates.
  • The size of these aggregates increases with increasing dendrimer generation.
  • The formation of discrete particles was observed.

Conclusions:

  • Nucleated aggregation of galectin-3 can be regulated by the choice of nucleating polymer.
  • These findings enhance the understanding of galectin-3 binding and function.
  • Provides insights into the role of sugar-binding proteins in biological processes.