The collagen model peptide Ac-(Hyp-Gly-Pro)2-NMe2 with the replacement of Pro3 by azPro in the middle of the sequence well adopted polyproline II structures with RMSD = 0.6 Å in water.
Introduction of CF3-oxazolidines in polyproline type II foldamers maintains PPII helicity, non-cytotoxicity and stability towards proteolysis. The CF3 groups enhanced hydrophobicity and are used as easy-to-handle 19F NMR probes.
We investigate short peptides and their propensity to form specific secondary structures. We show that the propensity might start to appear in sequences as short as several (3-11) amino acids.
We expand the synthesis and structural characterization of polyproline tri-helix macrocycle nanoscaffolds. The proposed structural model predicts the ligand locations against the target protein for nanomedicine development.
We show that using oligoprolines enables us to create defined metal-peptidic cages with three metal-binding motifs, forming a new family of Pd3L4 dual-cavity anisotropic ‘peanut’ cages.