Inhibition of α-helix-mediated protein-protein interactions using designed molecules.

By V. Azzarito, Kérya Long, N. Murphy, Andrew J. Wilson. Nature Chemistry, 2013

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Small-molecule inhibitors of protein-protein interactions: progressing toward the reality. (2014, background): “This type of epitope is also highly amenable to stabilized peptide approaches (Azzarito et al., 2013; Bernal et al., 2010; Boersma et al., 2012; Chang et al., 2013).”
Getting Across the Cell Membrane: An Overview for Small Molecules, Peptides, and Proteins (2015, background): “In some instances, cyclization by covalently linking internal residues has been proposed to increase permeability by changing the peptide’s α-helical content [127].”
Comprehensive Analysis of Loops at Protein-Protein Interfaces for Macrocycle Design (2014, unknown): “5,6 Numerous strategies are also available for mimicking or structurally stabilizing α -helices, including side-chain-to-side-chain crosslinks, backbone-to-backbone crosslinks, backbone replacements using unnatural residues such as β -amino acids, and non-peptidic scaffolds such as terphenyls or…”