Modulating glycosidase degradation and lectin recognition of gold glyconanoparticles

被引：29

作者：

Barrientos, Africa G. ^{[1
]}

de la Fuente, Jesus M. ^{[1
]}

Jimenez, Marta ^{[2
]}

Solis, Dolores ^{[2
]}

Javier Canada, F. ^{[3
]}

Martin-Lomas, Manuel ^{[1
,4
]}

Penades, Soledad ^{[1
,4
]}

机构：

[1] CSIC, IIQ, Lab Glyconanotechnol, E-41080 Seville, Spain

[2] CSIC, Inst Quim Fis Rocasolano, Madrid, Spain

[3] CSIC, Ctr Invest Biol, Madrid, Spain

[4] CIC BiomaGUNE CIBER BNN, San Sebastian 2009, Guipuzcoa, Spain

来源：

CARBOHYDRATE RESEARCH | 2009年 / 344卷 / 12期

关键词：

Gold glyconanoparticles; Glycosidases; Lectins; Multivalent presentation; Molecular recognition; AB-TYPE LECTIN; CELL-SURFACE; MULTIVALENT INTERACTIONS; MISTLETOE LECTIN; PROTEIN-BINDING; LIGAND DENSITY; NANOPARTICLES; INHIBITORS; GLYCOPROTEIN; AFFINITY;

D O I：

10.1016/j.carres.2009.04.029

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Glyconanoparticles (GNPs) are water-soluble carbohydrate-functionalized gold nanoclusters with a promising potential to serve as versatile tools in studies ranging from basic chemical glycobiology to clinical applications. In this paper we evaluate the influence of ligand density and presentation on the recognition by protein receptors by examining the interaction of lactose-functionalized GNPs with two different galactose-specific carbohydrate-binding proteins: an enzyme, Escherichia coli beta-galactosidase, and a lectin, Viscum album agglutinin. The results suggest that the proper selection of ligand densities and spacers in GNP functionalization is an important requisite to match the topological requirements of the target receptor while escaping glycosidase degradation. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：1474 / 1478

页数：5

共 71 条

[1] Lactose-containing starburst dendrimers:: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties [J].

André, S ;

Ortega, PJC ;

Perez, MA ;

Roy, R ;

Gabius, HJ .

GLYCOBIOLOGY, 1999, 9 (11) :1253-1261

[2] Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets [J].

André, S ;

Kaltner, H ;

Furuike, T ;

Nishimura, SI ;

Gabius, HJ .

BIOCONJUGATE CHEMISTRY, 2004, 15 (01) :87-98

[3]

André S, 2001, CHEMBIOCHEM, V2, P822, DOI 10.1002/1439-7633(20011105)2:11<822::AID-CBIC822>3.0.CO

[4]

2-W

[5] Calix[n]arene-based glycoclusters:: Bioactivity of thiourea-linked galactose/lactose moieties as inhibitors of binding of medically relevant lectins to a glycoprotein and cell-surface glycoconjugates and selectivity among human adhesion/growth-regulatory galectins [J].

Andre, Sabine ;

Sansone, Francesco ;

Kaltner, Herbert ;

Casnati, Alessandro ;

Kopitz, Juergen ;

Gabius, Hans-Joachim ;

Ungaro, Rocco .

CHEMBIOCHEM, 2008, 9 (10) :1649-1661

[6] High-avidity, low-affinity multivalent interactions and the block to polyspermy in Xenopus laevis [J].

Arranz-Plaza, E ;

Tracy, AS ;

Siriwardena, A ;

Pierce, JM ;

Boons, GJ .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (44) :13035-13046

[7] Gold glyconanoparticles:: Synthetic polyvalent ligands mimicking glycocalyx-like surfaces as tools for glycobiological studies [J].

Barrientos, AG ;

de la Fuente, JM ;

Rojas, TC ;

Fernández, A ;

Penadés, S .

CHEMISTRY-A EUROPEAN JOURNAL, 2003, 9 (09) :1909-1921

[8] SYNTHESIS OF THIOL-DERIVATIZED GOLD NANOPARTICLES IN A 2-PHASE LIQUID-LIQUID SYSTEM [J].

BRUST, M ;

WALKER, M ;

BETHELL, D ;

SCHIFFRIN, DJ ;

WHYMAN, R .

JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS, 1994, (07) :801-802

[9] Control of multivalent interactions by binding epitope density [J].

Cairo, CW ;

Gestwicki, JE ;

Kanai, M ;

Kiessling, LL .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (08) :1615-1619

[10]

CANADA J, UNPUB

← 1 2 3 4 5 6 7 8 →