title: Inhibition binding studies of glycodendrimer-lectin interactions using surface plasmon resonance.
abstract: Understanding protein-carbohydrate interactions is essential for elucidating biological pathways and cellular mechanisms but is often difficult due to the prevalence of multivalent interactions. Here, we evaluate the multivalent glycodendrimer framework as a means to describe the inhibition potency of multivalent mannose-functionalized dendrimers using surface plasmon resonance (SPR). Using highly robust, mannose-functionalized dithiol self-assembled monolayers on gold surfaces, we found that glycodendrimers were efficient inhibitors of protein-carbohydrate interactions. IC(50) values ranging from 260 nM to 13 nM were obtained for mannose-functionalized dendrimers with Concanavalin A.
authors.affiliation: Department of Chemistry and Biochemistry, 103 Chemistry and Biochemistry Building, Montana State University, Bozeman, MT 59717.
authors.forename: Kristian H
authors.initials: KH
authors.lastname: Schlick
authors.forename: Mary J
authors.initials: MJ
authors.lastname: Cloninger
references.citation: Chem Biol. 1997 Feb;4(2):97-104
references.pmid: 9190292
references.citation: Biochemistry. 1995 Apr 25;34(16):5685-95
references.pmid: 7727428
references.citation: Anal Chem. 2008 Apr 1;80(7):2556-63
references.pmid: 18321131
references.citation: Trends Biotechnol. 2004 Oct;22(10):524-30
references.pmid: 15450746
references.citation: Chem Rev. 2002 Feb;102(2):555-78
references.pmid: 11841254
references.citation: J Phys Chem B. 2005 Nov 24;109(46):21532-8
references.pmid: 16853796
references.citation: FEBS Lett. 2006 May 1;580(10):2402-8
references.pmid: 16616922
references.citation: Biosens Bioelectron. 2007 Jun 15;22(12):2983-8
references.pmid: 17261364
references.citation: Biochemistry. 1994 Feb 8;33(5):1149-56
references.pmid: 8110746
references.citation: J Am Chem Soc. 2005 May 4;127(17):6192-7
references.pmid: 15853323
references.citation: Angew Chem Int Ed Engl. 1998 Nov 2;37(20):2754-2794
references.pmid: 29711117
references.citation: Anal Chem. 2008 Dec 1;80(23):9265-71
references.pmid: 19551990
references.citation: Chemistry. 2009 Dec 7;15(47):13232-40
references.pmid: 19859921
references.citation: Chem Rev. 2002 Feb;102(2):387-429
references.pmid: 11841248
references.citation: J Am Chem Soc. 2009 Dec 16;131(49):17765-7
references.pmid: 19919053
references.citation: Org Lett. 2002 Jan 10;4(1):7-10
references.pmid: 11772077
references.citation: Anal Chem. 2003 Aug 1;75(15):348A-353A
references.pmid: 14572026
references.citation: J Am Chem Soc. 2003 Jul 23;125(29):8820-6
references.pmid: 12862477
references.citation: Anal Chem. 1999 Feb 15;71(4):777-90
references.pmid: 10051846
references.citation: J Am Chem Soc. 2005 May 25;127(20):7328-9
references.pmid: 15898778
references.citation: Carbohydr Res. 1991 Jun 25;213:69-77
references.pmid: 1933954
references.citation: Glycoconj J. 2004;21(3-4):89-95
references.pmid: 15483375
references.citation: Biosens Bioelectron. 2008 Sep 15;24(1):60-5
references.pmid: 18455919
references.citation: J Mol Recognit. 2006 Nov-Dec;19(6):478-534
references.pmid: 17125150
references.citation: Science. 2001 Mar 23;291(5512):2357-64
references.pmid: 11269316
references.citation: Bioconjug Chem. 2006 Sep-Oct;17(5):1125-35
references.pmid: 16984119
references.citation: Glycoconj J. 2000 Jul-Sep;17(7-9):543-51
references.pmid: 11421347
references.citation: Cancer Metastasis Rev. 2001;20(3-4):245-77
references.pmid: 12085965
references.citation: Bioconjug Chem. 2004 Mar-Apr;15(2):349-58
references.pmid: 15025531
references.citation: Chembiochem. 2004 Jun 7;5(6):740-64
references.pmid: 15174156
references.citation: Anal Chem. 2010 Mar 1;82(5):1712-9
references.pmid: 20112971