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

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...

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Bibliographic Details
Published in:RSC advances 2018-04, Vol.8 (26), p.14597-1462
Main Authors: Oliver, Martin, Gadais, Charlène, García-Pindado, Júlia, Teixidó, Meritxell, Lensen, Nathalie, Chaume, Grégory, Brigaud, Thierry
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Summary: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. The incorporation of trifluoromethylated proline analogues in the tripeptide PLG enhances its hydrophobicity and promotes passive diffusion transport.
ISSN:2046-2069
DOI:10.1039/c8ra02511h