New paper on peptoid helix folding from the Voelz Lab

Nature relies on the remarkable folding properties of proteins and nucleic acids to perform vital chemical work. Not surprisingly, synthetic chemists have long set their sights on developing non-natural molecules—called “foldamers”—that can harness similar folding properties for a number of diverse applications including nanomaterials, biotherapeutics, and chemical catalysts.

Peptoids (N-substituted oligoglycines) are bio-inspired synthetic heteropolymers that can fold into a number of diverse structural scaffolds. In a new paper by Mukherjee et al., we report on improved simulation potentials that better model peptoid helices, a key motif for peptide mimics. We then use a statistical mechanical helix-coil model to examine the thermodynamic forces that drive helix formation. We find that, unlike peptides, peptoid helices can increase their entropy upon folding, indicating that steric bulk of plays a large role in stabilizing helices. These findings will help future efforts in computational peptoid design.

Just Accepted manuscript: