End-capped α-helices as modulators of protein function

Examination of complexes of proteins with other biomolecules reveals that proteins tend to interact with partners via folded subdomains, in which the backbone possesses secondary structure. α-Helices, the largest class of protein secondary structures, play fundamental roles in a multitude of highly specific protein–protein and protein–nucleic acids interactions. Herein, we describe the potential of a helix nucleation strategy to afford modulators of protein–protein interactions.