| Summary: | The work done in this thesis aims to visualize multivalent binding events of proteins and their ligands, more specifically lectins and sugar moieties. This visualization is done by single channel recording (SCR) via stochastic sensing. Herein, the binding is studied at a single molecular level. Two mannose moieties are covalently connected by linker molecules to an ion channel forming protein, forming bivalent mannopores. These bivalent mannopores are used in a SCR set-up, wherein different lectins are added to study their binding behaviour. The lectins differ in their valency, with monovalent, bivalent, trivalent and tetravalent lectins being used. For each of these lectins, a binding model was derived that shows the dynamic nature of a multivalent binding event. This work shows that lectin-sugar binding is much more dynamic than previous theories would suggest.
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