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- W2092438962 abstract "The specificity of helix-induction in the 15-mers of poly-L-glutamic acid and poly-L-lysine by 2,2,2-trifluoroethanol (TFE) was investigated by circular dichroism (CD), NMR, and FTIR at three pH values: 2, 7, and 13. TFE was observed to promote the induction of helical conformation in poly-L-glutamic acid at pH 2.0, and pH 7.0. Similarly, TFE induces helical conformation in poly-L-lysine at pH 7.0 and pH 13. At pH 7.0, the helical conformation was induced in both poly-L-glutamic acid and poly-L-lysine only at higher concentrations of TFE (> 70 % v/v). At lower concentrations of the fluorinated alcohol, very little or no effect was observed in the backbone conformation of the homopolypeptides. 1H-15N HSQC spectra (obtained at 15N natural abundance, at pH 7.0) of the homopolypeptides showed that profound conformational changes occur in the backbone of the polypeptide chains in higher concentrations of TFE. Analysis of the 2D NMR data in conjunction with those obtained using Far UV CD and FTIR revealed that the helix conformation induced at higher concentrations of TFE is non-specific. Additionally, the role of the charged amino and carboxyl groups at the ends of the peptides were studied to determine if these groups affect helix induction by TFE. 15-mers of poly-L-glutamic acid and poly-L-lysine were synthesized from amide resins and their C-terminals were acetylated. The protected poly-L-glutamic acid and poly-L-lysine were titrated with TFE at pH 2, 7 and 13, and the secondary structures were determined using CD: no significant difference was found when compared to the non-protected homopolypeptides. The results obtained in this study clearly question the validity of structures of short peptides characterized in high concentrations of organic solvents." @default.
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- W2092438962 date "2009-02-01" @default.
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- W2092438962 title "Specificity Of The Helical Conformation Induced By 2, 2, 2, Trifluoroethanol" @default.
- W2092438962 doi "https://doi.org/10.1016/j.bpj.2008.12.3053" @default.
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