Interaction of Fluorescently Labeled Triethyleneglycol and Peptide Derivatives with β-Cyclodextrin

• Published in: Chemphyschem 2014-02, Vol.15 (3), p.444-457
• Main Authors: Alouini , Mohamed-Anis, Moustoifa, El-Farouck, Rubio-Albenque, Sandra, Berthelot, Thomas, Fery-Forgues , Suzanne, Déléris, Gérard
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; beta-Cyclodextrins - chemistry; Biological and medical sciences; Chemical Sciences; Coumarins - chemistry; dyes/pigments; Ethylene Glycol - chemistry; fluorescence; Fluorescence Resonance Energy Transfer; Fluorescent Dyes - chemistry; FRET; Fundamental and applied biological sciences. Psychology; inclusion compounds; Material chemistry; Miscellaneous; Models, Molecular; peptides; Peptides - chemistry; Proteins
• ISSN: 1439-4235; 1439-7641
• DOI: 10.1002/cphc.201301032

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. FRET‐active inclusion complexes: Linear and cyclic peptides are labeled with a donor–acceptor pair of coumarin dyes. These compounds form inclusion complexes with β‐cyclodextrins (β‐CDs) and retain most of their Förster resonance energy transfer (FRET) properties. This paves the way for the subsequent use of doubly labeled peptides in analytical devices that are designed to measure the activity of matrix metalloproteinases.