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Probing the Outstanding Local Hydrophobicity Increases in Peptide Sequences Induced by Incorporation of Trifluoromethylated Amino Acids
Author(s) -
Gadais Charlène,
Devillers Emmanuelle,
Gasparik Vincent,
Chelain Evelyne,
Pytkowicz Julien,
Brigaud Thierry
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800088
Subject(s) - tripeptide , chemistry , peptide , amino acid , stereochemistry , oligopeptide , lipophilicity , isoleucine , rational design , combinatorial chemistry , organic chemistry , leucine , biochemistry , nanotechnology , materials science
In order to achieve accurate determination of the local hydrophobicity increases in peptide sequences produced by incorporation of trifluoromethylated amino acids (TfmAAs), the chromatographic hydrophobicity indexes ( ϕ 0 ) of three series of tripeptides containing three unnatural trifluoromethylated amino acids have been measured and compared with those of their non‐fluorinated analogues. The hydrophobic contribution of each fluorinated amino acid was quantified by varying the position and the protection of ( R )‐ and ( S )‐α‐trifluoromethylalanine (TfmAla), ( R )‐trifluoromethylcysteine (TfmCys), and ( S )‐trifluoromethionine (TFM) in a short peptide sequence. As a general trend, strong increases in hydrophobicity were precisely measured, even exceeding the high hydrophobic contribution of the natural amino acid isoleucine. This study validates the incorporation of trifluoromethylated amino acids into peptide sequences as a rational strategy for the fine‐tuning of hydrophobic peptide–protein interactions.