Complexation behavior of cucurbit[6]uril with short polypeptides |
| |
Authors: | Hans-Jü rgen Buschmann, Lucia Mutihac, Radu-Cristian Mutihac,Eckhard Schollmeyer |
| |
Affiliation: | aDeutsches Textilforschungszentrum Nord-West e.V., Adlerstrasse 1, D-47798 Krefeld, Germany bUniversity of Bucharest, Department of Analytical Chemistry, 4-12 Blvd. Regina Elisabeta, 703461 Bucharest, Romania |
| |
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. |
| |
Keywords: | Cucurbit[6]uril Peptides Complexes Calorimetric titration |
本文献已被 ScienceDirect 等数据库收录! |
|