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Carbohydrate recognition specificity

This biosensor consists of two surface-tethered components. The biorecognition element can be an antibody (Section 19-5), DNA, RNA, or carbohydrate with specific affinity for analyte. A structural analog of the analyte is bound to a flexible arm adjacent to the recognition element. In the absence of analyte, the tethered analog binds to the recognition element. [Pg.402]

Aromatic amino acid side chains and their orientation play a crucial role in carbohydrate binding their specific interaction with the ligand is ubiquitous to CBM carbohydrate recognition. The side chains of tryptophan, tyrosine, and, less commonly, phenylalanine, form the hydrophobic platforms in CBM-binding sites, which can be planar, twisted, or form a sandwich (Boraston et al, 2004). [Pg.209]

Hildebrand A, Schaedlich A, Rothe U, Neubert RHH (2002) Sensing specific adhesion of liposomal and micellar systems with attached carbohydrate recognition structures at lectin surfaces. J Colloid Interface Sci 249 274—281... [Pg.158]

McGreal EP, Rosas M, Brown GD, Zamze S, Wong SYC, Gordon S, Martinez-Pomares L, Taylor PR. The carbohydrate-recognition domain of Dectin-2 is a C-type lectin with specificity for high mannose. Glycobiology 2006 16 422-430. [Pg.50]

The applications of synthetic, multivalent carbohydrate derivatives range from their use as inhibitors to biosensors [211] to cell type-specific targeting agents [81,212,213]. Further investigations into the fundamental issues of protein-carbohydrate recognition will provide additional tools and insights for the modulation of physiological processes. [Pg.2518]


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See also in sourсe #XX -- [ Pg.318 ]




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Carbohydrate-specificity

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