Photophysical properties of porphyrinoid sensitizers non-covalently bound to host molecules; models for photodynamic therapy

Lang, Kamil; Mosinger, Jiří; Wagnerová, D. M.

doi:10.1016/j.ccr.2004.02.004

Cited by 415 publications

(365 citation statements)

References 174 publications

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“…BSA has hydrophobic pockets which bind non-covalently to a range of drugs 31 and luminescent labels, 32 and binding reduces the aggregation of porphyrin 165 photosensitisers. 33 A marked increase in emission intensity is observed following titration with BSA for all the dimers except P 2 and P 2 -Suc. The protein-assisted disaggregation process is accelerated by heating.…”

Section: Linear Absorption and Fluorescence Spectramentioning

confidence: 89%

Photophysical properties and intracellular imaging of water-soluble porphyrin dimers for two-photon excited photodynamic therapy

et al. 2009

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Section: Linear Absorption and Fluorescence Spectramentioning

confidence: 89%

Photophysical properties and intracellular imaging of water-soluble porphyrin dimers for two-photon excited photodynamic therapy

et al. 2009

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“…At present, it is unclear whether extra-nuclear TMPyP freely diffuses in the cytosol or if it binds, for example, to proteins. 58,59 Upon irradiation of TMPyP in these respective intracellular domains, we are able to For these intracellular experiments, the rate constant that accounts for all channels of singlet oxygen removal, k rem , can be expressed as a sum of four terms (Eq. 4), those previously reported.…”

Section: When Incorporated Into Hela Cells Tmpyp Ultimately Tends Tomentioning

confidence: 99%

Singlet Oxygen in a Cell: Spatially Dependent Lifetimes and Quenching Rate Constants

2008

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Singlet molecular oxygen, O 2 (a 1 ∆ g ), can be created in a single cell from ground state oxygen, O 2 (X 3 Σ g -), upon focused laser irradiation of an intracellular sensitizer. This cytotoxic species can subsequently be detected by its 1270 nm phosphorescence (a 1 ∆ g → X 3 Σ g -) with subcellular spatial resolution. The singlet oxygen lifetime determines its diffusion distance and, hence, the intracellular volume element in which singlet-oxygen-initiated perturbation of the cell occurs. In this study, the time-resolved phosphorescence of singlet oxygen produced by the sensitizers chlorin (Chl) and 5,10,15,20-tetrakis(N-methyl-4-pyridyl)-21H,23H-porphine (TMPyP) was monitored. These molecules localize in different domains of a living cell. The data indicate that (i) the singlet oxygen lifetime and (ii) the rate constant for singlet oxygen quenching by added NaN 3 depend on whether Chl or TMPyP was the photosensitizer.These observations likely reflect differences in the chemical and physical constituency of a given subcellular domain (e.g., spatially-dependent oxygen and NaN 3 diffusion coefficients) and, as such, are evidence that singlet oxygen responds to the inherent heterogeneity of a cell.Thus, despite a relatively long intracellular lifetime, singlet oxygen does not diffuse a great distance from its site of production. This is a consequence of an apparent intracellular viscosity that is comparatively large.3

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“…Hence, it is important to investigate how and to which extent it influences the photosensitized reactions. Conversely, upon binding, ligands can induce structural modifications in the proteins [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Translational and Rotational Motions of Albumin Sensed by a Non-Covalent Associated Porphyrin Under Physiological and Acidic Conditions: A Fluorescence Correlation Spectroscopy and Time Resolved Anisotropy Study

Andrade¹,

Costa²,

Borst

et al. 2008

J Fluoresc

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The interaction between a free-base, anionic watersoluble porphyrin, TSPP, and the drug carrier protein, bovine serum albumin (BSA) has been studied by time-resolved fluorescence anisotropy (TRFA) and fluorescence correlation spectroscopy (FCS) at two different pH-values. Both rotational correlation times and translational diffusion times of the fluorescent species indicate that TSPP binding to albumin induces very little conformational changes in the protein under physiological conditions. By contrast, at low pH, a biexponential decay is obtained where a short rotational correlation time (7 int =1.2 ns) is obtained, which is likely associated to wobbling movement of the porphyrin in the protein binding site. These physical changes are corroborated by circular dichroism (CD) data which show a 37% loss in the protein helicity upon acidification of the medium. In the presence of excess porphyrin formation of porphyrin Jaggregates is induced, which can be detected by timeresolved fluorescence with short characteristic times. This is also reflected in FCS data by an increase in molecular brightness together with a decrease in the number of fluorescent molecules passing through the detection volume of the sample.

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Photophysical properties of porphyrinoid sensitizers non-covalently bound to host molecules; models for photodynamic therapy

Cited by 415 publications

References 174 publications

Photophysical properties and intracellular imaging of water-soluble porphyrin dimers for two-photon excited photodynamic therapy

Photophysical properties and intracellular imaging of water-soluble porphyrin dimers for two-photon excited photodynamic therapy

Singlet Oxygen in a Cell: Spatially Dependent Lifetimes and Quenching Rate Constants

Translational and Rotational Motions of Albumin Sensed by a Non-Covalent Associated Porphyrin Under Physiological and Acidic Conditions: A Fluorescence Correlation Spectroscopy and Time Resolved Anisotropy Study

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