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• W2056525098 startingPage "79" @default.
• W2056525098 abstract "The binding properties of cucurbit[6]uril towards various peptides have been investigated in acidic aqueous solution. Stability constants and thermodynamic values of the complex formation between following peptides: glycyl-l-alanine, l-leucyl-l-valine, glycyl-l-asparagine, l-leucyl-l-phenylalanine, l-leucyl-l-tryptophan, glycyl-l-histidine, l-glutathione reduced (γ-l-glutamyl-l-cysteinyl-glycine, GSH), and dl-leucyl-glycyl-dl-phenylalanine) with cucurbit[6]uril in aqueous formic acid (50%, v/v) have been calculated from calorimetric titrations. From these results it can be seen that the peptides form exclusion complexes with cucurbit[6]uril. Due to the polar peptide bond they are not included within the hydrophobic cavity of cucurbit[6]uril. The complex formation is favoured by entropic contributions. The release of water molecules from the polar amino groups of the peptides and the carbonyl groups of cucurbituril are responsible." @default.
• W2056525098 created "2016-06-24" @default.
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• W2056525098 date "2005-06-01" @default.
• W2056525098 modified "2023-10-12" @default.
• W2056525098 title "Complexation behavior of cucurbit[6]uril with short polypeptides" @default.
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• W2056525098 doi "https://doi.org/10.1016/j.tca.2005.01.002" @default.
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