| Non-covalent self-assembly is a fundamental process that directs the structural and functional diversity of biomolecules. The interplay of non-covalent interactions that stabilize and guide the fidelity of these structures includes hydrogen bonding, pi-pi stacking, metal-ligand coordination, hydrophobic, electrostatic and van der Waals forces.;Protein-binding agents have been developed using architectures found in Nature as non-covalent scaffolds. Specifically, deoxyribonucleotides have been used as scaffolds to orient, in a well-defined way, functional groups for protein active site and protein surface recognition.;Chapter 1 describes non-covalent self-assemblies in Nature and the progress made by synthetic chemists in emulating the principles of this process through recognition-encoded elements. The applications of deoxyribonucleotides as functional molecules in nanobiotechnology are also surveyed.;Chapter 2 to 4 of this thesis evaluate the protein-binding properties of functionalized duplexes, quadruplexes and pentaplexes respectively. An organic fragment-conjugated duplex library has been tested for binding to streptavidin and effective bidentate ligands have been identified. Chapter 3 explores the versatility of higher-ordered DNA structures in the design of tetradentate ligands for protein surface recognition. Finally, the abiotic self-assembly properties of isoguanine nucleobases have been exploited in the design of a pentadentate ligand for protein recognition in Chapter 4. |
