Interaction of indole derivatives and tryptophan peptides with interfaces of sodium dodecyl sulfate micelles

✍ Scribed by Takeyoshi Imamura; Kazue Konishi; Katsutoshi Konishi

• Publisher: John Wiley and Sons
• Year: 2006
• Tongue: English
• Weight: 146 KB
• Volume: 12
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.741

✦ Synopsis

Abstract

The free energies of transfer for indole and tryptophan derivatives and pentapeptides having single tryptophan residues from aqueous to sodium dodecyl sulfate (SDS) micellar phases have been systematically studied using the conventional method of ultraviolet absorption spectrophotometry. The free energies for the position isomers of methyl indoles varied depending on the substitution positions. Thus, the contribution of the methyl group to the binding affinity of the 4‐methyl indole to the micelle was about twice that of the 2‐ and 7‐methyl indoles. The free energy changes with the introduction of halogen groups to the indole rings were correlated to the nonpolar water‐accessible surface area (Δ__A__~np~) of the halogen moieties, which were regarded as hydrophobic. The relationships followed straight lines passing through the origins. Position dependence having tendencies similar to the methyl indoles was observed among the magnitudes of the slopes of the straight lines. These results strongly suggest that the indole rings of the derivatives residing in the micellar interface regions direct their imino moieties NH toward the micellar surfaces. Experiments using model tryptophan pentapeptides showed that the magnitude of free energy change per methylene unit of an alkyl amino acid residue in the pentapeptide increased with elongation of the alkyl moiety and was not a constant value as reported for various alkyl compounds. When the peptides distribute to the SDS micelles, the peptide backbones are anchored in aqueous phases and the amino acid side chains in the interfaces extend their alkyl groups toward the micellar centers. Thus, the free energy changes can be connected to the positions of the alkyl groups of the amino acid residues in the micelles. Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.