Association of Protein Helices and Assembly of Foldamers: Stories in Membrane and Aqueous Environments

摘要: Solvents play an important role in association and assembly of molecules. Here we studied solvent effects on proteins organic chemicals different contexts. First, X-ray crystal structures show that helix dimers membrane- water-soluble have distinct behaviors packing sequence selection. Transmembrane are stabilized by compact hydrogen bonding between small residues. Meanwhile, utilize hydrophobic residues for irrespective the size interface tight rare. Secondly, apply results learned above to a complex system which designed protein binds single-walled carbon-nanotube aqueous environments. Previous designs hexameric helical bundles utilized leucine alanine make two helix-helix interfaces. Our molecular dynamics simulations showed alanine-comprising is much more labile than leucine-comprising one. This result can be interpreted scarcity soluble as mentioned above. Thus stable modular interfaces employed design peptides binding carbon-nanotubes with higher affinities. Lastly, describe serendipitous discovery crystalline framework structure amphiphilic triarylamide foldamer. Foldamers peptide-like polymers non-natural monomers arranged defined chain length able adopt protein-like secondary tertiary structures. In contrast traditional metal-organic frameworks, exploit strong directional coordination solvents, herein built up from combination noncovalent hydrophobic, hydrogen-bonded, electrostatic interactions solution. The honeycomb geometry each cubicle truncated octahedron. A new supramolecular synthon, π-π stacking encompassed, was discovered structure. Through NMR experiments probed oligomeric states foldamer early stages prior crystallization. hierarchic discussed terms synthons engineering.