concanavalin-a and triethylene-glycol

Multivalency is a key, ubiquitous phenomenon in nature characterized by a complex combination of binding mechanisms, with special relevance in carbohydrate-lectin recognition. Herein we introduce an original surface plasmon resonance kinetic approach to analyze multivalent interactions that has been validated with dendrimers as monodisperse multivalent analytes binding to lectin clusters. The method, based on the analysis of early association and late dissociation phases of the sensorgrams provides robust information of the glycoconjugate binding efficiency and real-time structural data of the binding events under the complex scenario of the glyco-cluster effect. Notably, it reveals the dynamic nature of the interaction and offers experimental evidence on the contribution of binding mechanisms.

Topics: Algorithms; Concanavalin A; Dendrimers; Gallic Acid; Kinetics; Linear Models; Models, Chemical; Polyethylene Glycols; Surface Plasmon Resonance

Experiments by Surface Plasmon Resonance (SPR) illustrate the relevance of lectin density for the reliable evaluation of binding efficiencies in surface-based multivalent carbohydrate recognition. The difference between affinity data obtained by solution and surface-based experiments is also stressed.

Topics: Concanavalin A; Dendrimers; Gallic Acid; Mannose; Molecular Structure; Polyethylene Glycols; Surface Properties

Densely packed co-adsorbed ultrathin mono molecular layers of short tri(ethylene glycol)-alkanethiolate (for repelling proteins) and maltoside terminated alkanethiolate (for capturing lectin) provided an extremely high signal to noise ratio surface: the repelling molecules, which had two different functions (highly flexible-hydrophilic arm and rigid packing tail group), worked as "nano barriers" in the recognition monolayer.

Topics: Adsorption; Alkanes; Animals; Cattle; Concanavalin A; Peptides; Polyethylene Glycols; Sensitivity and Specificity; Sulfhydryl Compounds