Silaproline helical mimetics selectively form an all-trans PPII helix

Chemistry. 2014 Oct 27;20(44):14240-4. doi: 10.1002/chem.201404820. Epub 2014 Sep 11.

Abstract

The polyproline II helix (PPII) is increasingly recognized as an important element in peptide and protein structures. The discovery of pertinent PPII peptidomimetics is of great interest to tune physical properties of the targeted structure. A series of silaproline oligomers from dimer to pentamer were synthesized. CD studies, NMR spectroscopy and molecular modeling revealed that the ribbon preferentially populates the polyproline type II secondary structure in both [D]chloroform and [D4 ]MeOH. The characteristics of this new lipophilic PPII-like helix were determined.

Keywords: NMR spectroscopy; helix; molecular modeling; peptidomimetics; silaproline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomimetic Materials / chemistry
  • Circular Dichroism
  • Models, Molecular
  • Organosilicon Compounds / chemistry*
  • Peptides / chemistry*
  • Proline / analogs & derivatives*
  • Proline / chemistry
  • Protein Structure, Secondary

Substances

  • Organosilicon Compounds
  • Peptides
  • silaproline
  • polyproline
  • Proline