This review discusses the structural features, biological significance, detection methods, and biomimetic applications of Polyproline II helices, emphasizing recent advances in characterization techniques and their roles in supramolecular assembly.
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.
Using molecular dynamics simulations, this study examined AFGP8 and its proline mutants binding to ice planes. Proline maintains the rigidity of AFGP8 and PPII helix, enabling a hydrophobic–hydrophilic pattern that stabilizes ice binding.