Fluorescent amino acids as reporter systems in peptido-cyclodextrin inclusion compounds

Eddaoudi, Mohamed; Parrot‐Lopez, Hélène; Lamotte, Sophie; Ficheux, Damien; Prognon, Patrice; Coleman, Anthony W.

doi:10.1039/p29960001711

Cited by 23 publications

(10 citation statements)

References 6 publications

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“…Fluorescent labeling has recently emerged as a highly promising tool for diverse bioanalytical applications including in vitro and in vivo imaging, 61 high-throughput screening, 62 proteomics, 62 diagnostics, 63 single biomolecule spectroscopy, 64 HPLC control 65 and the exploration of protein conformations. 66 Many markers incorporate an amino acid to tag the fluorescent moiety.…”

Section: Fluorescent Amino Acids and Peptidesmentioning

confidence: 99%

Chiral Acylation with N-(Protected α-Aminoacyl)benzotriazoles for Advantageous Syntheses of Peptides and Peptide Conjugates

Katritzky¹,

Angrish²,

Todadze³

2009

Synlett

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N-(Protected a-aminoacyl)benzotriazoles are efficient intermediates for N-and O-aminoacylation. These intermediates enable fast preparations of biologically relevant peptides and peptide conjugates in high yields and purity, under mild reaction conditions, with full retention of the original chirality. The developed methodology allows simple solution-and solid-phase preparative techniques to generate complex peptides and peptide conjugates and serves as a platform for generating diverse medicinal chemistry building block libraries involving amino acid and heterocyclic moieties crucial for drug development.

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Section: Fluorescent Amino Acids and Peptidesmentioning

confidence: 99%

Chiral Acylation with N-(Protected α-Aminoacyl)benzotriazoles for Advantageous Syntheses of Peptides and Peptide Conjugates

Katritzky¹,

Angrish²,

Todadze³

2009

Synlett

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“…18 In particular, for 5, a one-dimensional supramolecular array with a helically extended polymeric structure has been found to form in the solid state by repetition of intermolecular inclusion. 18 Fluorescent artificial cyclodextrins have received considerable attention in sensory, 20 biochemical 21 and photoelectronic 22 applications. The CDx cavity offering a binding site and a fluorophore acting as a signaling unit with a linkage group are indispensable for substrate specific-responsive functions.…”

Section: Introductionmentioning

confidence: 99%

Fluorescent behaviour in hostâ€“guest interactions. Part 2.For Part 1 see ref. 16(b). Thermal and pH-dependent sensing properties of two geometric isomers of fluorescent amino-Î²-cyclodextrin derivatives

Nakashima

Takenaka

Higashi

et al. 2001

J. Chem. Soc., Perkin Trans. 2

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The fluorescent behaviour in aqueous solution of two types of amino-β-cyclodextrin (amino-β-CDx) isomers 1 and 2 bearing the naphthoamide group at the 1-and 2-position as a fluorescent-sensing unit was investigated using mainly fluorescence spectroscopy. The isomers 1 and 2 show both strong temperature-and pH-responsive photophysical properties in aqueous solution. The protonation of the amino groups of 1 and 2 in acidic media affects efficiently their fluorescence intensities. The equilibrium and thermodynamic quantities of the two-state equilibrium model for 1 and 2 have been determined spectrophotometrically. Solution NMR behaviour in a DMSO-D 2 O mixed solvent confirms the stereospecific relationship between the appended naphthalene fluorophore and the hydrophobic cavity of CDx. Restricted and/or flexible motion of the naphthalene moiety of 1 and 2 about the bond between the amide group and the amino group at the C-6 carbon atom in the CDx ring is evident from the NMR studies. The potential application of 1 to anion sensing is also discussed. 2096

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“…In contrast, fluorescent tags are introduced as an additional moiety to the molecule, by a variety of strategies. [5][6][7][8][9][10] Derivatives of rhodamine, fluorescein 11,12 and coumarin 13,14 are widely used as fluorescent markers for peptides and other biomolecules. Xanthenes such as rhodamines, fluoresceins and Alexa dyes are advantageously bright; however, drawbacks of existing derivatives in reporting protein conformational changes include (i) relatively long, flexible linkers between the probe and protein, which questions whether the probe motions faithfully mirror the motions of the residue to which it is attached, and (ii) multiple charges and relatively large surface areas, which can perturb local structure or motion, and inhibit labeling at certain positions.…”

mentioning

confidence: 99%

“…The many bioanalytical applications of fluorescently labeled proteins include in vitro and in vivo imaging, 6,23 high-throughput screening, 24 proteomics, [24][25][26] diagnostics, 9,27,28 single biomolecule spectroscopy, 26,29 HPLC control 30 and exploring protein conformations. 7 Probes for studying protein dynamics and electrostatics should be (i) sensitive to the state of hydrogen bonding in the solvent environment 31 and (ii) readily incorporated regiospecifically at the C-or the N-terminus of a protein.…”

mentioning

confidence: 99%

Chiral N-(Coumarin-3-ylcarbonyl)-α-amino Acids: Fluorescent Markers for Amino Acids and Dipeptides

Katritzky¹,

Narindoshvili²,

Angrish³

2008

Synthesis

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benzotriazole has been coupled with free amino acids, N-terminal-protected lysines and dipeptides to afford fluorescent amino acids and dipeptides (76-89% yield) with retention of original chirality. N a -and N e -Coumarinlabeled lysines are obtained by simple, two-step procedures. N a -Cbz-N e -(Coumarin-3-ylcarbonyl)-L-lysine is demonstrated to be an optically active fluorescent marker for labeling amino acids in solutionphase syntheses.The imaging of living cells is a big challenge in cell biology. Understanding the nature and dynamics of cellular events in living organisms is assisted by imaging cell components such as the nucleic acids, proteins and metabolites. Fluorescent markers are the visualization tools most commonly used, particularly fluorescent tagging with organic fluorophores 1 or green fluorescent protein (GFP). 2 Highly sensitive fluorescence derivatization techniques 3 are gaining an increasing share of the analytical world market, becoming competitive with, for example, radioimmunoassay. 4Radioactive labeling of peptides usually involves the introduction of a radiolabeled amino acid as part of the natural structure of the peptide. In contrast, fluorescent tags are introduced as an additional moiety to the molecule, by a variety of strategies. 5-10 Derivatives of rhodamine, fluorescein 11,12 and coumarin 13,14 are widely used as fluorescent markers for peptides and other biomolecules. Xanthenes such as rhodamines, fluoresceins and Alexa dyes are advantageously bright; however, drawbacks of existing derivatives in reporting protein conformational changes include (i) relatively long, flexible linkers between the probe and protein, which questions whether the probe motions faithfully mirror the motions of the residue to which it is attached, and (ii) multiple charges and relatively large surface areas, which can perturb local structure or motion, and inhibit labeling at certain positions. 7,13 Coumarins (benzopyran-2-ones), the largest class of laser dyes for the blue-green region, 14-22 are highly sensitive. They have provided the most commercially acceptable categories of fluorescent derivatives with the advantages of an extended spectral range, high emission quantum yield, photostability and good solubility in many solvents.The many bioanalytical applications of fluorescently labeled proteins include in vitro and in vivo imaging, 6,23 high-throughput screening, 24 proteomics, 24-26 diagnostics, 9,27,28 single biomolecule spectroscopy, 26,29 HPLC control 30 and exploring protein conformations. 7Probes for studying protein dynamics and electrostatics should be (i) sensitive to the state of hydrogen bonding in the solvent environment 31 and (ii) readily incorporated regiospecifically at the C-or the N-terminus of a protein.The use of an amino acid as a fluorescent chromophore offers a good possibility to synthesize fluorescent peptides by solid-phase peptide synthesis (SPPS).Previously, enantioselective syntheses of coumarincontaining amino acids have been carried out by the diastereoselective...

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Fluorescent amino acids as reporter systems in peptido-cyclodextrin inclusion compounds

Cited by 23 publications

References 6 publications

Chiral Acylation with N-(Protected α-Aminoacyl)benzotriazoles for Advantageous Syntheses of Peptides and Peptide Conjugates

Chiral Acylation with N-(Protected α-Aminoacyl)benzotriazoles for Advantageous Syntheses of Peptides and Peptide Conjugates

Fluorescent behaviour in hostâ€“guest interactions. Part 2.For Part 1 see ref. 16(b). Thermal and pH-dependent sensing properties of two geometric isomers of fluorescent amino-Î²-cyclodextrin derivatives

Chiral N-(Coumarin-3-ylcarbonyl)-α-amino Acids: Fluorescent Markers for Amino Acids and Dipeptides

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