Glycodendrimers: tools to explore multivalent galectin-1 interactions
| Autor: | Mary J. Cloninger, Jonathan M. Cousin |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
animal structures
Nanoparticle dendrimer Full Research Paper Human prostate lcsh:QD241-441 lcsh:Organic chemistry Dynamic light scattering DU145 Competitive binding Dendrimer otorhinolaryngologic diseases Fluorescence microscope galectin-1 multivalent lcsh:Science glycodendrimer Chemistry nanoparticle Organic Chemistry Combinatorial chemistry stomatognathic diseases Galectin-1 Biophysics lcsh:Q |
| Zdroj: | Beilstein Journal of Organic Chemistry Beilstein Journal of Organic Chemistry, Vol 11, Iss 1, Pp 739-747 (2015) |
| ISSN: | 1860-5397 |
| DOI: | 10.3762/bjoc.11.84 |
| Popis: | Four generations of lactose-functionalized polyamidoamine (PAMAM) were employed to further the understanding of multivalent galectin-1 mediated interactions. Dynamic light scattering and fluorescence microscopy were used to study the multivalent interaction of galectin-1 with the glycodendrimers in solution, and glycodendrimers were observed to organize galectin-1 into nanoparticles. In the presence of a large excess of galectin-1, glycodendrimers nucleated galectin-1 into nanoparticles that were remarkably homologous in size (400–500 nm). To understand augmentation of oncologic cellular aggregation by galectin-1, glycodendrimers were used in cell-based assays with human prostate carcinoma cells (DU145). The results revealed that glycodendrimers provided competitive binding sites for galectin-1, which diverted galectin-1 from its typical function in cellular aggregation of DU145 cells. |
| Databáze: | OpenAIRE |
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