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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†
research-article
Martin Oliver ,
Charlène Gadais ,
Júlia García-Pindado ,
Meritxell Teixidó ,
Nathalie Lensen
,
Grégory Chaume
,
Thierry Brigaud
18 April 2018
17 April 2018
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Abstract
The synthesis of four CF 3-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 CF 3 group, Tfm-AAs can also promote passive diffusion transport.
Abstract
The incorporation of trifluoromethylated proline analogues in the tripeptide PLG enhances its hydrophobicity and promotes passive diffusion transport.
