Peptides are found in most cells in the body. They are these polymers made from alpha-amino acids. Many diseases can be traced back to malfunctions of these polymers. Therefore, these compounds will have great scope as pharmaceuticals.

Unfortunately, they can be recognized and therefore degraded. So, it would be of great interest to make some compounds that would mimic these peptides, but not be recognizable by the body. Some of the most studied mimics are beta peptides, where you have an extra carbon atom in the backbone,

and these peptoids, where you have moved the side chain to the nitrogen. For this project, we are working on this very novel combination of these two, where you both have the extra carbon atom and you have the side chain on the nitrogen. One of the things that we would very much like to mimic is the folding of these molecules,

which is one of the reasons for the great selectivity of peptides. And this is done by hydrogen bonding. Unfortunately, in these peptides, there are no hydrogen bond donors, yet they still display some secondary structure, some of them even stable.

So, what we are trying to find out is what's stabilizing these structures. And it has been proposed that it is either the oxygen lone pair that is interacting with the carbonyl group, or with the aryl groups of the side chains.

What these change is this amide bond, which can be thought of as a double bond. So, what we would like to do is we will try to control this equilibrium by substituting different things in the backbone, thereby being able to control the secondary structure.