Myriad biological processes are governed by chemical reactions that occur on cell surfaces. In the first part of this work, a novel approach to direct biological processes that occur at the surface of artificial materials is described. A multi-faceted strategy has been developed to construct ¿interfacial biomaterials¿ that mediate specific biological processes via increased cellular adhesion to medically-relevant materials. A phage display selection strategy was developed to identify peptides that show increased affinity for natural and artificial substrates. In the second part, the molecular basis of protein¿carbohydrate binding is considered. Ligands displaying lactose epitopes were constructed to investigate their aggregative properties towards full¿length and truncated galectin¿3. ITC studies with full¿length protein shows a greater than two¿fold enhancement in affinity for the bivalent ligand compared to monovalent ligand. This behavior demonstrates that protein-protein interactions and aggregation are the primary cause for affinity increases observed with polyvalent saccharide ligands, and unambiguously establishes a molecular basis for the cluster glycoside effect.
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James A. Parise Jr, PhD, is an Instructor and the Manager of the Organic Chemistry Laboratories at Duke University in Durham, North Carolina. He received his PhD in organic chemistry at Duke University in 2007 under the direction of Eric Toone and did his postdoctoral work with David Lawrence at the University of North Carolina at Chapel Hill.
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Seller: AHA-BUCH GmbH, Einbeck, Germany
Taschenbuch. Condition: 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. Seller Inventory # 9783639097993
Seller: preigu, Osnabrück, Germany
Taschenbuch. Condition: 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. Seller Inventory # 101690710
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