Binding to protein surfaces by supramolecular multivalent scaffolds

被引：82

作者：

Martos, Vera ^{[1
,2
]}

Castreno, Pilar ^{[1
]}

Valero, Julian ^{[1
,3
]}

de Mendoza, Javier ^{[1
,2
]}

机构：

[1] Inst Chem Res Catalonia ICIQ, Tarragona 43007, Spain

[2] Univ Autonoma Madrid, E-28049 Madrid, Spain

[3] Univ Rovira & Virgili, Tarragona 43007, Spain

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2008年 / 12卷 / 06期

关键词：

D O I：

10.1016/j.cbpa.2008.08.024

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：

Multivalency plays a pivotal role in biological recognition, particularly at protein-protein and protein-carbohydrate interaction sites. Scaffolds of diverse structure, flexibility, and valency are gaining increasing biomedical importance in the development of artificial multivalent ligands for these interfaces. Relevant examples range from small C-4 symmetric calix[4]arenes and porphyrin ligands, which may achieve nanomolar affinity for protein surfaces of pharmaceutical interest, to large-sized dendrimers that provide promising adherence-inhibition for toxins and other relevant lectins. In addition, highly flexible supramolecular platforms like rotaxanes and polymers have been proposed as challenging alternatives to more rigid designs. Finally, nanoparticles are being exploited for this aim as they present important advantages from the biological and synthetic points of view.

引用

页码：698 / 706

页数：9

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