ISBN: 9783639097993 - molecular interactions at the chemistry-biology interface: the design of interfacial biomaterials and the modulation of galectin¿3 aggregation with multivalent saccharide ligands (3 resultados)

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  • Idioma: Inglés

    Editorial: VDM Verlag Dr. Müller, 2008

    3639097998 / 9783639097993

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    Librería: preigu, Osnabrück, Alemaniapreigu

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    Taschenbuch. Condición: Neu. MOLECULAR INTERACTIONS AT THE CHEMISTRY-BIOLOGY INTERFACE | The Design of Interfacial Biomaterials and the Modulation of Galectin 3 Aggregation With Multivalent Saccharide Ligands | James Parise | Taschenbuch | Englisch | VDM Verlag Dr. Müller | EAN 9783639097993 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.…

  • Idioma: Inglés

    Editorial: VDM Verlag Dr. M ller, 2008

    3639097998 / 9783639097993

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    Librería: Mispah books, Redhill, SURRE, Reino UnidoMispah books

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    Condición: Usado - Como Nuevo

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    paperback. Condición: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

  • Idioma: Inglés

    Editorial: VDM Verlag Dr. Müller, 2008

    3639097998 / 9783639097993

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    Librería: AHA-BUCH GmbH, Einbeck, AlemaniaAHA-BUCH GmbH

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    EUR 66,55

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    Taschenbuch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Myriad biological processes are governed by chemicalreactions that occur on cell surfaces. In the firstpart of this work, a novel approach to directbiological processes that occur at the surface ofartificial materials is described. A multi-facetedstrategy has been developed to construct interfacialbiomaterials that mediate specific biologicalprocesses via increased cellular adhesion tomedically-relevant materials. A phage displayselection strategy was developed to identify peptidesthat show increased affinity for natural andartificial substrates. In the second part, themolecular basis of protein carbohydrate binding isconsidered. Ligands displaying lactose epitopes wereconstructed to investigate their aggregativeproperties towards full length and truncatedgalectin 3. ITC studies with full length proteinshows a greater than two fold enhancement in affinityfor the bivalent ligand compared to monovalentligand. This behavior demonstrates thatprotein-protein interactions and aggregation are theprimary cause for affinity increases observed withpolyvalent saccharide ligands, and unambiguouslyestablishes a molecular basis for the clusterglycoside effect.…