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Multivalent scaffolds induce galectin-3 aggregation into nanoparticles.

ABSTRACT: Galectin-3 meditates cell surface glycoprotein clustering, cross linking, and lattice formation. In cancer biology, galectin-3 has been reported to play a role in aggregation processes that lead to tumor embolization and survival. Here, we show that lactose-functionalized dendrimers interact with galectin-3 in a multivalent fashion to form aggregates. The glycodendrimer-galectin aggregates were characterized by dynamic light scattering and fluorescence microscopy methodologies and were found to be discrete particles that increased in size as the dendrimer generation was increased. These results show that nucleated aggregation of galectin-3 can be regulated by the nucleating polymer and provide insights that improve the general understanding of the binding and function of sugar-binding proteins.

SUBMITTER: Goodman CK

PROVIDER: S-EPMC4142985 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Multivalent scaffolds induce galectin-3 aggregation into nanoparticles.

Goodman Candace K CK Wolfenden Mark L ML Nangia-Makker Pratima P Michel Anna K AK Raz Avraham A Cloninger Mary J MJ

Beilstein journal of organic chemistry 20140710

Galectin-3 meditates cell surface glycoprotein clustering, cross linking, and lattice formation. In cancer biology, galectin-3 has been reported to play a role in aggregation processes that lead to tumor embolization and survival. Here, we show that lactose-functionalized dendrimers interact with galectin-3 in a multivalent fashion to form aggregates. The glycodendrimer-galectin aggregates were characterized by dynamic light scattering and fluorescence microscopy methodologies and were found to ...[more]

PMID: 25161713

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