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

The synthesis of four CF -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 an...

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Published in:RSC advances 2018-01, Vol.8 (26), p.14597-14602
Main Authors: Oliver, Martin, Gadais, Charlène, García-Pindado, Júlia, Teixidó, Meritxell, Lensen, Nathalie, Chaume, Grégory, Brigaud, Thierry
Format: Article
Language:English
Subjects:
Amino acids
Chemical Sciences
Chemistry
Hydrophobicity
Medicinal Chemistry
Peptides
Proline
Transport
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cited_by cdi_FETCH-LOGICAL-c440t-968bf6d1f0136c19eb163e70521392773029a7f069a65998610837ebccc4b39f3
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container_issue 26
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container_title RSC advances
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creator Oliver, Martin
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Brigaud, Thierry
description The synthesis of four CF -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 group, Tfm-AAs can also promote passive diffusion transport.
doi_str_mv 10.1039/c8ra02511h
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subjects Amino acids
Chemical Sciences
Chemistry
Hydrophobicity
Medicinal Chemistry
Peptides
Proline
Transport
title 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
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