The dysregulation of cell signaling pathways can lead to the development of diseases such as cancer and Alzheimer's disease. Signaling proteins implicated in the pathogenesis of these particular diseases contain WW domains that specifically bind polyproline type II (PPII) helices comprised of trans-amide bonds in the helix backbone. Thus, molecules that emulate PPII helices could be used as biological probes for gaining insight into the progression of these diseases. Peptoids (N-substituted glycine oligomers) could be especially useful for probing WW domain signaling because they are structurally similar to polyprolines, form rigid structures, and exhibit biostability. However, peptoids typically fold into PPI helices (comprised of cis-amides) instead of PPII helices. Incorporating thioamides into peptoids could generate a preference for trans-amides and PPII helix formation by strengthening n-pi* interactions within the peptoid backbone. Progress towards the development of a solid-phase synthetic method for constructing thiopeptoids will be presented.Figure 1. General structure of a thiopeptoid.

Synthesis and characterization of thiopeptoids as potential biological probes?

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.