Glycodendrimers: tools to explore multivalent galectin-1 interactions

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...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Jonathan M. Cousin [verfasserIn] Mary J. Cloninger [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Schlagwörter:	dendrimer galectin-1 glycodendrimer multivalent nanoparticle

Übergeordnetes Werk:	In: Beilstein Journal of Organic Chemistry - Beilstein-Institut, 2005, 11(2015), 1, Seite 739-747
Übergeordnetes Werk:	volume:11 ; year:2015 ; number:1 ; pages:739-747

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3762/bjoc.11.84

Katalog-ID:	DOAJ056170661

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allfieldsSound	10.3762/bjoc.11.84 doi (DE-627)DOAJ056170661 (DE-599)DOAJ082c96d7cdb04e7c8d7e79cbdbed0649 DE-627 ger DE-627 rakwb eng QD241-441 Jonathan M. Cousin verfasserin aut Glycodendrimers: tools to explore multivalent galectin-1 interactions 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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. dendrimer galectin-1 glycodendrimer multivalent nanoparticle Science Q Organic chemistry Mary J. Cloninger verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 11(2015), 1, Seite 739-747 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:11 year:2015 number:1 pages:739-747 https://doi.org/10.3762/bjoc.11.84 kostenfrei https://doaj.org/article/082c96d7cdb04e7c8d7e79cbdbed0649 kostenfrei https://doi.org/10.3762/bjoc.11.84 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2015 1 739-747
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callnumber-first	Q - Science
author	Jonathan M. Cousin
spellingShingle	Jonathan M. Cousin misc QD241-441 misc dendrimer misc galectin-1 misc glycodendrimer misc multivalent misc nanoparticle misc Science misc Q misc Organic chemistry Glycodendrimers: tools to explore multivalent galectin-1 interactions
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topic_title	QD241-441 Glycodendrimers: tools to explore multivalent galectin-1 interactions dendrimer galectin-1 glycodendrimer multivalent nanoparticle
topic	misc QD241-441 misc dendrimer misc galectin-1 misc glycodendrimer misc multivalent misc nanoparticle misc Science misc Q misc Organic chemistry
topic_unstemmed	misc QD241-441 misc dendrimer misc galectin-1 misc glycodendrimer misc multivalent misc nanoparticle misc Science misc Q misc Organic chemistry
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title	Glycodendrimers: tools to explore multivalent galectin-1 interactions
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title_full	Glycodendrimers: tools to explore multivalent galectin-1 interactions
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title_sort	glycodendrimers: tools to explore multivalent galectin-1 interactions
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title_auth	Glycodendrimers: tools to explore multivalent galectin-1 interactions
abstract	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.
abstractGer	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.
abstract_unstemmed	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.
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title_short	Glycodendrimers: tools to explore multivalent galectin-1 interactions
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