Guest post from Dr. Greg Bowman, UC Berkeley
Prof. Vince Voelz’s lab has published an exciting paper on their recent successes with predicting the structures of protein-like molecules called peptoids (here). Peptoids are similar to proteins but with a rearrangement in their chemistry (see example below). Their similarity to proteins allows peptoids to function like proteins. However, the alteration in peptoid chemistry relative to proteins effectively makes them invisible to parts of the immune system designed to recognize foreign proteins. Therefore, peptoids are an attractive option for drug design. To fully realize this potential, we need to be able to predict the structures of peptoids and design them to perform specific functions. The Voelz lab’s work demonstrates that computer simulations can provide this sort of information by presented predicted structures of a number of peptoids along with experimental structures confirming the accuracy of their predictions (see example below).
Peptide vs. peptoid chemistry. In peptoids, a group of atoms (called R) is moved from a carbon to an adjacent nitrogen (N).
An example of one of the Voelz lab's predicted structures (in green) overlaid with the experimental structure (in white).