The importance of the left-handed polyproline II (PPII) helical conformation has recently become apparent. This conformation generally is involved in two important functions: protein-protein interactions and structural integrity. The PPII helix is believed to be the dominant conformation for many proline-rich regions of peptides and proteins. In particular PPII are major features of collagens.
In our laboratory, an original proline analogue has been synthesized: the 4,4-dimethylsilaproline, denoted silaproline (Sip)1 . The presence of dimethylsilyl group confers to silaproline a higher lipophilicity as well as an improved resistance to biodegradation.
Recently we developed a gram scale synthesis of enantiomerically pure Sip, requiring resolution of the racemate by chiral high performance liquid chromatography (HPLC)2.
With this new starting material, our aim was to construct polysilaproline polymers to investigate physico chemical properties and modifications of PPII structure.
In this study monodisperses homopolypeptides have been synthesized by peptide coupling in solution, polydisperses homopolypeptides have been prepared by ring opening polymerization of N-carboxyanhydrides (ROP). These peptides have been characterized by RMN, MALDI-Tof and circular dichroism.
*Correspondance : florine@univ-montp2.fr