Designing functional proteins and enzymes has proven to be very challenging. Many of the reported examples in literature utilize strategic placement of hydrophobic residues to direct the tertiary folding of designed proteins in water. This strategy, however, fails in nonpolar solvents as hydrophobic collapse can no longer provide cue to the folding sequence.We propose to take a different approach to this problem in which strong and specific hydrogen bonding units, introduced in the primary sequence of peptides, replace the hydro-phobic collapse. We envision that large enthalpic gain from pairing of these strong hydrogen bonding units in a nonpolar environment can control and guide the folding process. Herein, we report the synthesis and incorporation, of two supramolecular unnatural amino acids with specific array of hydrogen bonding acceptors and donors in a series of peptides and peptoids and their effect on the secondary structure.

Design and application of unnatural supramolecular amino acids as templates for peptide folding

243rd National Meeting (2012)

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