Learning outcomes

This course examines the fundamentals of supramolecular chemistry, the domain of chemistry beyond that of molecules, in biological contexts. The discipline focuses on the chemical systems made up of a discrete number of assembled molecular subunits or components. Important concepts that have been demonstrated by supramolecular chemistry include molecular self-assembly, biomolecular folding, molecular recognition, host-guest chemistry, and molecular architectures. Students develop an understanding of the driving forces of supramolecular associations and how to exploit them for applications in biotechnology and biomedicine.

Program

Concepts. Reversible non-covalent interactions between molecules, including hydrogen bonding, metal coordination, hydrophobic forces, van der Waals forces, pi-pi interactions, electrostatics. Cation , anion, and neutral molecule binding.
Biological supramolecular systems: protein-protein and protein-ligand complexes, nucleic acids, viruses, membranes, cells.
Methods. Fluorescence spectroscopy, Calorimetry, NMR spectroscopy.
Self-assembly and self-organization. Thermodynamics of self-assembly. Template effects. Protein aggregation, fibril formation.
Molecular recognition. Host-guest chemical systems. Receptor-ligand complexes. Lock and key model. Pre-organization and complementarity. Dynamic effects and allosteric binding. Rational drug design. Protein-protein interaction inhibitors. Supramolecular antibiotics.
Catalysis. Biocatalysis. Template-directed synthesis. Encapsulation systems for catalysis. Catalytic systems. Enzyme mimics.
Molecular transport and delivery. Encapsulation and targeted release mechanisms. Liposomal drug carriers. Cyclodextrins.
Biomolecule-nanoparticle interactions. The biomolecular corona of nanoparticles. Nanoparticle effects on protein stability and structure. Hybrid nanosystems. Nanoparticle functionalization with biomolecules.

Examination Methods

Oral exam