Interaction of Fluorescently Labeled Triethyleneglycol and Peptide Derivatives with β‐Cyclodextrin. Issue 3 (8th January 2014)

• Record Type: Journal Article
• Authors: Alouini , Mohamed‐Anis; Moustoifa, El‐Farouck; Rubio‐Albenque, Sandra; Berthelot, Thomas; Fery‐Forgues , Suzanne; Déléris, Gérard
• Is Part Of: Chemphyschem. Volume 15:Issue 3(2014)
• Page Start: 444
• Page End: 457
• Publication Date: 2014-01-08
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.05
• DOI: 10.1002/cphc.201301032
• Languages: English
• ISSNs: 1439-4235

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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.</p> </abstract>