Probing the Outstanding Local Hydrophobicity Increases in Peptide Sequences Induced by Incorporation of Trifluoromethylated Amino Acids
| Autor: | Julien Pytkowicz, Emmanuelle Devillers, Thierry Brigaud, Evelyne Chelain, Charlène Gadais, Vincent Gasparik |
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| Rok vydání: | 2018 |
| Předmět: |
chemistry.chemical_classification
Alanine Halogenation 010405 organic chemistry Stereochemistry Organic Chemistry Peptide Tripeptide 010402 general chemistry 01 natural sciences Biochemistry 0104 chemical sciences Amino acid Hydrophobic effect Methionine chemistry Molecular Medicine Amino Acid Sequence Cysteine Isoleucine Peptides Hydrophobic and Hydrophilic Interactions Molecular Biology Peptide sequence |
| Zdroj: | ChemBioChem. 19:1026-1030 |
| ISSN: | 1439-4227 |
| DOI: | 10.1002/cbic.201800088 |
| Popis: | 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 (ϕ0 ) 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. |
| Databáze: | OpenAIRE |
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