Photobinding of ketoprofen in vitro and ex vivo

Moser, Jill; Sarabia, Zaideth; Minter, Helen; Lovell, W.W.; Henegouwen, Gerard M. J. Beijersbergen van

doi:10.1016/s1011-1344(00)00111-1

Cited by 15 publications

(8 citation statements)

References 9 publications

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“…The drug or its photoproducts containing the BZPH chromophore should be able to abstract hydrogen from the C-H bonds of amino acids or to participate in electron-transfer processes, producing photoactive cross-linking reactions or protein photooxidations, as described for BZPH (74)(75)(76). In fact, photobinding of KP or KP1 to HSA has been observed (77,78).…”

Section: Proteinsmentioning

confidence: 99%

Photoreactivity of the Nonsteroidal Anti-inflammatory 2-Arylpropionic Acids with Photosensitizing Side Effects¶

Boscá

Marín

Miranda

2007

Photochemistry and Photobiology

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The photoreactivity of the nonsteroidal anti-inflammatory 2-arylpropionic acids benoxaprofen, carprofen, naproxen, ketoprofen, tiaprofenic acid, and suprofen is reviewed with special emphasis on fundamental photophysical and photochemical properties. The absorption and emission properties of the excited states of these drugs as well as their main photodegradation routes are summarized. The photochemical mechanisms are discussed on the basis of product studies and detection of short-lived intermediates by means of laser flash photolysis. After dealing with the unimolecular processes, attention is focused on the photosensitized reactions of key biomolecules, such as lipids, proteins or nucleic acids. Finally, a short section on the photobiological effects on simple biological models is also included. Although some earlier citations are included, the literature coverage is in general limited to the last decade.

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Section: Proteinsmentioning

confidence: 99%

Photoreactivity of the Nonsteroidal Anti-inflammatory 2-Arylpropionic Acids with Photosensitizing Side Effects¶

Boscá

Marín

Miranda

2007

Photochemistry and Photobiology

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“…The interest in this system was inspired by the fact that KP, a very important non steroidal anti-inflammatory drug (NSAID) administrated as the racemate, is pharmacologically active only as the S(+) enantiomer; moreover KP bears a photoreactive chromophore, the benzoylphenyl moiety, [5][6][7][8][9] capable of inducing biological photosensitization and photoallergic effects, [10][11][12] the latter reactions being mediated by covalent photoaddition to proteins. [13][14][15] Serum albumin represent the major transport medium for this drug in plasma and is considered a good model for the investigation of drug-protein binding and reactivity. In this context we previously studied binding and photochemistry of KP enantiomers within the BSA 16,17 and HSA 18 matrices using circular dichroism (CD) and fluorescence.…”

Section: Introductionmentioning

confidence: 99%

Chiral recognition of 2-(3-benzoylphenyl)propionic acid (ketoprofen) by serum albumin: an investigation with microcalorimetry, circular dichroism and molecular modelling

Monti

Ottani

Manoli

et al. 2009

Phys. Chem. Chem. Phys.

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The interaction of enantiomeric ketoprofen (KP) with BSA and HSA was studied by isothermal titration calorimetry (ITC). Affinity constants and thermodynamic parameters for complexation in two main protein sites were determined. Affinity constants for both proteins are generally lower for S(+)- than for R(-)-KP. Large enthalpic contributions to Gibbs free energy are compensated by large negative entropic terms for S(+) in the BSA-subdomain IIIA and HSA-subdomain IIA. The lowest energy BSA complexes of both enantiomers were structurally characterized by combining molecular mechanics (MM) and molecular dynamics (MD) with circular dichroism (CD). Comparison of quantum mechanically calculated rotational strengths with the CD signals of the complexes supported the structures. These allowed to identify the main interactions of the KP enantiomers with surrounding amino acids at short distances, that limit significantly KP mobility in both sites. In the primary binding site S(+) is close to Tyr 409 in subdomain IIIA (Sudlow site II), and R(-) is close to Trp 212 and His 240 in subdomain IIA (Sudlow site I). The same sites are involved in the formation of 2:1 complexes. The equilibrium structures are characterized by marked geometrical distortion of KP.

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“…151 In competition with photodecarboxylation, photobinding of KPF to the proteins has been reported. 139,154,155 This is interesting from the photobiological point of view, as covalent photoadduct formation is the origin of the clinically reported photoallergy.…”

Section: Intraprotein Photoreactivitymentioning

confidence: 99%

Photoactive assemblies of organic compounds and biomolecules: drug–protein supramolecular systems

et al. 2014

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Photobinding of ketoprofen in vitro and ex vivo

Cited by 15 publications

References 9 publications

Photoreactivity of the Nonsteroidal Anti-inflammatory 2-Arylpropionic Acids with Photosensitizing Side Effects¶

Photoreactivity of the Nonsteroidal Anti-inflammatory 2-Arylpropionic Acids with Photosensitizing Side Effects¶

Chiral recognition of 2-(3-benzoylphenyl)propionic acid (ketoprofen) by serum albumin: an investigation with microcalorimetry, circular dichroism and molecular modelling

Photoactive assemblies of organic compounds and biomolecules: drug–protein supramolecular systems

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