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Silaproline Helical Mimetics Selectively Form an All‐ trans PPII Helix
Author(s) -
Martin Charlotte,
Legrand Baptiste,
Lebrun Aurélien,
Berthomieu Dorothée,
Martinez Jean,
Cavelier Florine
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201404820
Subject(s) - polyproline helix , pentamer , peptidomimetic , chemistry , helix (gastropod) , dimer , circular dichroism , stereochemistry , nuclear magnetic resonance spectroscopy , peptide , crystallography , organic chemistry , biochemistry , biology , ecology , snail
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 [D 4 ]MeOH. The characteristics of this new lipophilic PPII‐like helix were determined.