|
|||||
|
|
Interaction of Fluorescently Labeled Triethyleneglycol and Peptide Derivatives with β‐Cyclodextrin |
|
| Authors: | Dr. Mohamed‐Anis Alouini Dr. El‐Farouck Moustoifa Dr. Sandra Rubio‐Albenque Dr. Thomas Berthelot Dr. Suzanne Fery‐Forgues Prof. Gérard Déléris |
| Affiliation: | 1. SynVec, ADERA, 146 rue Léo Saignat, 33000 Bordeaux Cedex, (France);2. FRE3396 CNRS, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, (France);3. Laboratory of Chemistry of Surfaces and Interfaces, CEA Saclay, IRAMIS/SPCSI, 91191, Gif‐sur‐Yvette Cedex, (France);4. Université de Toulouse, ITAV‐USR 3505, 31106 Toulouse (France);5. CNRS, ITAV‐USR3505, 31106 Toulouse (France);6. Université de Toulouse, IMRCP‐UMR 5623, 31062 Toulouse (France);7. CNRS, IMRCP‐UMR5623, 31062 Toulouse (France) |
| Abstract: | A triethyleneglycol (TEG) chain, a linear peptide, and a cyclic peptide labeled with 7‐methoxycoumarin‐3‐carboxylic acid (MC) and 7‐diethylaminocoumarin‐3‐carboxylic acid (DAC) were used to thoroughly study Förster resonance energy transfer (FRET) in inclusion complexes. 1H NMR evidence was given for the formation of a 1:1 inclusion complex between β‐cyclodextrin (β‐CD) and the fluorophore moieties of model compounds. The binding constant was 20 times higher for DAC than for MC derivatives. Molecular modeling provided additional information. The UV/Vis absorption and fluorescence properties were studied and the energy transfer process was quantified. Fluorescence quenching was particularly strong for the peptide derivatives. The presence of β‐CDs reduced the FRET efficiency slightly. Dye‐labeled peptide derivatives can thus be used to form inclusion complexes with β‐CDs and retain most of their FRET properties. This paves the way for their subsequent use in analytical devices that are designed to measure the activity of matrix metalloproteinases. |
| Keywords: | dyes/pigments fluorescence FRET inclusion compounds peptides |