Human serum albumin mutants complexed Mn(iii) protoporphyrin IX as superoxide dismutase mimics

Kato, Ryunosuke; Kobayashi, Yuya; Akiyama, Motofusa; Komatsu, Teruyuki

doi:10.1039/c3dt51418h

Cited by 10 publications

(8 citation statements)

References 41 publications

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“…The main biological defence system to mitigate SO is superoxide dismutase (SOD) enzymes. 144,145 SODs are enzymes that catalyse the dismutation of SO to hydrogen peroxide and oxygen very efficiently. SOD contains a redoxactive metal with the capability of oxidizing and reducing SO.…”

Section: Substituted Fluorinated Porphyrinoids For Application In Matmentioning

confidence: 99%

Fluorinated porphyrinoids as efficient platforms for new photonic materials, sensors, and therapeutics

et al. 2016

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Porphyrinoids are robust heterocyclic dyes studied extensively for their applications in medicine and as photonic materials because of their tunable photophysical properties, diverse means of modifying the periphery, and the ability to chelate most transition metals. Commercial applications include their use as phthalocyanine dyes in optical discs, porphyrins in photodynamic therapy, and as oxygen sensors. Most applications of these dyes require exocyclic moieties to improve solubility, target diseases, modulate photophysical properties, or direct the self-organization into architectures with desired photonic properties. The synthesis of the porphyrinoid depends on the desired application, but the de novo synthesis often involves several steps, is time consuming, and results in low isolated yields. Thus, the application of core porphyrinoid platforms that can be rapidly and efficiently modified to evaluate new molecular architectures allows researchers to focus on the design concepts rather than the synthesis methods, and opens porphyrinoid chemistry to a broader scientific community. We have focused on several widely available, commercially viable porphyrinoids as platforms: meso-perfluorophenylporphyrin, perfluoro-phthalocyanine, and meso-perfluorophenylcorrole. The perfluorophenylporphyrin is readily converted to the chlorin, bacteriochlorin, and isobacteriochlorin. Derivatives of all six of these core platforms can be efficiently and controllably made via mild nucleophilic aromatic substitution reactions using primary S, N, and O nucleophiles bearing a wide variety of functional groups. The remaining fluoro groups enhance the photo and oxidative stability of the dyes and can serve as spectroscopic signatures to characterize the compounds or in imaging applications using 19F NMR. This review provides an overview of the chemistry of fluorinated porphyrinoids that are being used as a platform to create libraries of photo-active compounds for applications in medicine and materials.

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Section: Substituted Fluorinated Porphyrinoids For Application In Matmentioning

confidence: 99%

Fluorinated porphyrinoids as efficient platforms for new photonic materials, sensors, and therapeutics

et al. 2016

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“…[11][12][13] The protein was reported to serve as a transporter for a variety of endogenous and exogenous compounds such as drugs, fatty acids and dyes in the bloodstream. [11][12][13] The protein was reported to serve as a transporter for a variety of endogenous and exogenous compounds such as drugs, fatty acids and dyes in the bloodstream.…”

Section: Introductionmentioning

confidence: 99%

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH₃)₂Cl₂(O₂CCH₂CH₂COOH)-(OCONHC₁₆H₃₃)] with serum albumin – thermodynamic and conformational investigations

Liu

Lang

et al. 2015

New J. Chem.

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In this paper, a potential anti-hepatoma Pt 4+ drug cis,cis,trans-[Pt(NH 3 ) 2 Cl 2 (O 2 CCH 2 CH 2 COOH)-(OCONHC 16 H 33 )] was synthesized and selected to investigate its binding to human serum albumin (HSA) by spectroscopy and molecular docking methods. Fluorescence spectra show that the Trp residue, the intrinsic fluorophore in HSA, was induced to a less hydrophobic microenvironment with the addition of the Pt 4+ compound, which induces the denaturation of HSA. Moreover, the fluorescence quenching mechanism was determined to be static quenching. The binding constant (K A ) and the number of binding sites (n) were calculated based on the results of fluorescence measurements. Circular dichroism (CD), Fourier transform infrared spectroscopy (FTIR) and three dimensional fluorescence spectroscopy proved that the Pt 4+ compound could slightly change the secondary structure and induce unfolding of the polypeptides of protein. Thermodynamic parameters indicate that the Pt 4+ compound binds to HSA through electrostatic attraction with one binding site. The molecular docking study indicated that parecoxib is embedded into site I (subdomain IIA) of HSA.

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“…When a porphyrin enters a living organism, it may combine with a protein such as HSA, and this will control its accumulation, distribution, and metabolism in the body. Therefore, there have been numerous studies on the interaction of porphyrins with HSA …”

Section: Introductionmentioning

confidence: 99%

“…Therefore, there have been numerous studies on the interaction of porphyrins with HSA. [32][33][34][35][36][37][38][39][40][41][42][43][44][45][46] 2-Chloronicotinic acid is a bioactive small molecule that has attracted much attention as a key precursor in the synthesis of pesticides and medicines. In the present work, 2chloronicotinic acid has been appended onto the porphyrin ring through 1,2-dibromoethane to afford free-base tailed porphyrins and Zn porphyrins.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Tailed Metalloporphyrins Modified with 2‐Chloronicotinic Acid and Interactions with Human Serum Albumin

Wang

Peng

Zhang

et al. 2017

Bulletin Korean Chem Soc

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Two kinds of free‐base tailed porphyrins modified with 2‐chloronicotinic acid and the corresponding Zn porphyrins have been synthesized. They have been characterized by elemental analysis and NMR, UV/Vis, fluorescence spectra, and infrared spectroscopies. Their configurations have been optimized through theoretical calculations. The fluorescence quantum yields were determined by a comparative method. The interactions between the Zn porphyrins and human serum albumin have been studied by means of fluorescence spectra. The experimental results showed that the interaction mechanism involved a combined fluorescence quenching process (static and dynamic quenching) and that the main driving force was hydrophobic in nature. Quenching constants, binding constants, thermodynamic parameters, and binding distances have been determined.

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Human serum albumin mutants complexed Mn(iii) protoporphyrin IX as superoxide dismutase mimics

Abstract: Genetically engineered human serum albumin (HSA) mutants complexed Mn(III) protoporphyrin IX (MnPP) in the haem pocket showed superoxide dismutase activity. Replacement of a proximal Tyr-161 by non-coordinating Leu caused a remarkable increase in enzyme activity.

Cited by 10 publications

References 41 publications

Fluorinated porphyrinoids as efficient platforms for new photonic materials, sensors, and therapeutics

Fluorinated porphyrinoids as efficient platforms for new photonic materials, sensors, and therapeutics

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH₃)₂Cl₂(O₂CCH₂CH₂COOH)-(OCONHC₁₆H₃₃)] with serum albumin – thermodynamic and conformational investigations

Synthesis of Tailed Metalloporphyrins Modified with 2‐Chloronicotinic Acid and Interactions with Human Serum Albumin

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Human serum albumin mutants complexed Mn(iii) protoporphyrin IX as superoxide dismutase mimics

Abstract: Genetically engineered human serum albumin (HSA) mutants complexed Mn(III) protoporphyrin IX (MnPP) in the haem pocket showed superoxide dismutase activity. Replacement of a proximal Tyr-161 by non-coordinating Leu caused a remarkable increase in enzyme activity.

Cited by 10 publications

References 41 publications

Fluorinated porphyrinoids as efficient platforms for new photonic materials, sensors, and therapeutics

Fluorinated porphyrinoids as efficient platforms for new photonic materials, sensors, and therapeutics

Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH3)2Cl2(O2CCH2CH2COOH)-(OCONHC16H33)] with serum albumin – thermodynamic and conformational investigations

Synthesis of Tailed Metalloporphyrins Modified with 2‐Chloronicotinic Acid and Interactions with Human Serum Albumin

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Binding of a potential anti-hepatoma drug cis,cis,trans-[Pt(NH₃)₂Cl₂(O₂CCH₂CH₂COOH)-(OCONHC₁₆H₃₃)] with serum albumin – thermodynamic and conformational investigations