Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States.

The construction of protein-sized synthetic chains that blend natural amino acids with artificial monomers to create so-called heterogeneous-backbones is a powerful approach to generate complex folds and functions from bio-inspired agents. A variety of techniques from structural biology commonly used to study natural proteins have been adapted to investigate folding in these entities. In NMR characterization of proteins, proton chemical shift is a straightforward to acquire, information-rich metric that bears directly on a variety of properties related to folding.

Solid phase syntheses of peptoid like arylureido compounds and sequencing of isobars without molecular encoding.

Arylureido-backbone containing peptoid-like trimers were prepared using the one-bead-one-compound approach. Isobaric molecules were synthesized from isocyanate precursors that contain alkyl halide handles at the ortho and para-positions in the phenyl ring. After chain extension with a primary amine, the piperazine-capped molecules were sequenced using tandem mass spectrometry and successfully identified based on their fragmentation pattern without a need for internal molecular encoding.