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Carbohydrate Microarrays for Lectin Characterization and Glyco-Epitope Identification

ABSTRACT: Lectins can also be classified according to their binding specificity or selectivity with carbohydrates. This type of classification is helpful for selection of lectins as structural probes in biomedical applications. This chapter summarizes the concept and the updated information regarding the specificity-based lectin classification. Lectins are functionally classified based on their relative binding reactivities with the structural units of carbohydrate or glyco-epitopes. They are grouped according to their monosaccharide specificities and then further sub-grouped based on their reactivities with more complex structures. Carbohydrate specificities of biomedically important lectins are classified into six groups according to their specificities to monosaccharides. The chapter introduces a practical platform of carbohydrate microarrays that is useful for lectin characterization and classification. Finally, the chapter discusses a few examples to illustrate the application of this technology in lectin-related experimental investigations.

SUBMITTER: Wang D

PROVIDER: S-EPMC7158280 | biostudies-literature | 2007 Jan

REPOSITORIES: biostudies-literature

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Project description:Monoliths of nanoporous gold (np-Au) were modified with self-assembled monolayers of octadecanethiol (C18-SH), 8-mercaptooctyl α-D-mannopyranoside (αMan-C8-SH), and 8-mercapto-3,6-dioxaoctanol (HO-PEG2-SH), and the loading was assessed using thermogravimetric analysis (TGA). Modification with mixed SAMs containing αMan-C8-SH (at a 0.20 mole fraction in the SAM forming solution) with either octanethiol or HO-PEG2-SH was also investigated. The np-Au monoliths modified with αMan-C8-SH bind the lectin Concanavalin A (Con A), and the additional mass due to bound protein was assessed using TGA analysis. A comparison of TGA traces measured before and after exposure of HO-PEG2-SH modified np-Au to Con A showed that the non-specific binding of Con A was minimal. In contrast, np-Au modified with octanethiol showed a significant mass loss due to non-specifically adsorbed Con A. A significant mass loss was also attributed to binding of Con A to bare np-Au monoliths. TGA revealed a mass loss due to the binding of Con A to np-Au monoliths modified with pure αMan-C8-SH. The use of mass losses determined by TGA to compare the binding of Con A to np-Au monoliths modified by mixed SAMs of αMan-C8-SH and either octanethiol or HO-PEG2-SH revealed that binding to mixed SAM modified surfaces is specific for the mixed SAMs with HO-PEG2-SH but shows a significant contribution from non-specific adsorption for the mixed SAMs with octanethiol. Minimal adsorption of immunoglobulin G (IgG) and peanut agglutinin (PNA) towards the mannoside modified np-Au monoliths was demonstrated. A greater mass loss was found for Con A bound onto the monolith than for either IgG or PNA, signifying that the mannose presenting SAMs in np-Au retain selectivity for Con A. TGA data also provide evidence that Con A bound to the αMan-C8-SH modified np-Au can be eluted by flowing a solution of methyl α-D-mannopyranoside through the structure. The presence of Con A proteins on the modified np-Au surface was also confirmed using atomic force microscopy (AFM). The results highlight the potential for application of carbohydrate modified np-Au monoliths to glycoscience and glycotechnology and demonstrate that they can be used for capture and release of carbohydrate binding proteins in significant quantities.

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Carbohydrate Microarrays for Lectin Characterization and Glyco-Epitope Identification

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