Trifluoromethylated proline analogues as efficient tools to enhance the hydrophobicity and to promote passive diffusion transport of the L-prolyl-L-leucyl glycinamide (PLG) tripeptide

Martin Oliver; Charlène Gadais; Júlia García-Pindado; Meritxell Teixidó; Nathalie Lensen; Grégory Chaume; Thierry Brigaud

doi:10.1039/C8RA02511H

This website uses cookies to give you the best user experience. If you continue without changing your settings we'll assume you are happy to receive all RSC cookies. You can change your cookie settings by navigating to our Privacy and Cookies page and following the instructions. These instructions are also obtainable from the privacy link at the bottom of any RSC page.

Lite Version|Standard version

Home > RSC Advances > Trifluoromethylated pro...

Trifluoromethylated proline analogues as efficient tools to enhance the hydrophobicity and to promote passive diffusion transport of the L-prolyl-L-leucyl glycinamide (PLG) tripeptide

Martin Oliver, Charlène Gadais, Júlia García-Pindado, Meritxell Teixidó, Nathalie Lensen, Grégory Chaume and Thierry Brigaud
RSC Adv., 2018,8, 14597-14602
DOI: 10.1039/C8RA02511H, Paper

Open Access Learn more..

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.

Download

PDF

Rich HTML

Abstract | Cited by

The synthesis of four CF₃-proline analogues of the PLG peptide is reported. Our results show that the incorporation of trifluoromethylated amino acids (Tfm-AAs) at the N-terminal position of a peptide significantly increases its hydrophobicity. In addition, depending on the relative configuration and the position of the CF₃ group, Tfm-AAs can also promote passive diffusion transport.

Graphical abstract: Trifluoromethylated proline analogues as efficient tools to enhance the hydrophobicity and to promote passive diffusion transport of the l-prolyl-l-leucyl glycinamide (PLG) tripeptide

Page: ^ Top

Terms & Conditions | Privacy and Cookies