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Synthesis of beta-polypeptides via ring-opening polymerization of beta-lactams The natural world is replete with complex molecules classified in general as biopolymers, which are proteins that govern essential processes of life and that have physical properties that render them capable of forming fantastic materials like spider silk and collagen. Proteins achieve these functions by folding into compact, well-ordered formations known as tertiary or quaternary structures, which in turn depend on the nature of the polypeptide's stable secondary structure such as alpha-helix, turns, and beta-sheets. The nature of the protein's complex tertiary structure is vital in directing its specific biological function. A nickel initiator that was developed by the Deming group for the polymerization of alpha- and beta-amino acid N-carboxyanhydride NCAs was attempted for the first time on beta-lactams yielding high molecular weight beta-polypeptides with quantitative conversion and in good purity. I report a brief summary of the work that was carried out in order to perform these polymerizations. I also provide some nuclear magnetic resonance (NMR) and infrared (IR) characterization data of beta-amino acids and beta-lactams synthesized and some preliminary conformational analysis data of the resulting beta-polypeptide, based on circular dichroism (CD) spectroscopy data. Return to the RISE 2000 project list |
