The specific sequence of monomers make proteins have amazingly precise 3D structures and special functions. Scientists have been trying to synthesize polymers with similar level of order and precision for application in medicine, catalysis and material sciences. Polypeptoids are structural mimics of polypeptides, and can be synthesized from diversified monomers with specific sequence. Originated for studying proteins, HP lattice model, in which only hydrophobic (H) and polar (P) monomers are considered, has been employed to predict folding behaviors of heteropolymer chains. We believe that hydrophobic sequence patterning in polymer chains is one of the most predominant determinants of folding a heteropolymer into a defined structure. Carrying this idea and based on HP model, we prepared polypeptoids with defined sequence by solid-phase synthesis from two monomers, hydrophobic N-isobutylglycine and polar N-(2-hydroxyethyl)glycine or N-(2-carboxyethyl)glycine monomers. Here we systematically evaluate the ability of HP peptoid 40-50mers of varying composition and sequence to fold into compact single-chain globular structures, and to catalyze simple chemical transformations.

Sequence effects on the chain folding and function of protein-like polypeptoids

248th National Meeting (2014)

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