Photoprocesses of chlorin e6 bound to lysozyme or bovin serum albumin

Zhang, Yazhou; Görner, Helmut

doi:10.1016/j.dyepig.2009.04.013

Cited by 14 publications

(9 citation statements)

References 46 publications

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“…It was found that a QD-Ce 6 complex is formed when a non-polar part of Ce 6 interacts with the hydrophobic part of QDs phospholipid coating [14,15], which is evidenced by a fluorescence band shift from 660 to 670 nm, analogous as for Ce 6 molecules present in the hydrophobic environment [13,[16][17][18].…”

Section: Discussionmentioning

confidence: 99%

Complexes of functionalized quantum dots and chlorin e<sub>6</sub> in photodynamic therapy

Rotomskis¹,

Valančiūnaitė²,

Skripka³

et al. 2013

Lith. J. Phys.

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Recently, it has been suggested that quantum dots (QDs) could be used in the photodynamic therapy of cancer as resonance energy donors for conventional porphyrin type photosensitizers. Here we present the results of the spectroscopic studies on the formation of a non-covalent complex between QDs and photosensitizer chlorin Ce 6 in an aqueous medium and in the presence of bovine serum albumin (BSA). Changes in the absorption and fluorescence spectra of QDs and Ce 6 revealed the formation of a QD-Ce 6 complex which occurs due to hydrophobic interaction between the nonpolar moiety of an amphiphilic photosensitizer and the hydrophobic part of the lipid-based coating of the QD. The photosensitizer conjugated with the QD could be indirectly excited by the Forster resonance energy transfer (FRET) from the QD to Ce 6 . The investigation on the capacity of such complex to generate 1 O 2 showed that the QD-Ce 6 complex irradiated by visible light is able to produce 1 O 2 more efficiently than QDs or Ce 6 taken separately. The photoinactivation of cells incubated with the QD-Ce 6 complex and irradiated in the spectral region where the photosensitizer does not absorb provided evidence that such complex could induce FRET-mediated cell destruction.

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Section: Discussionmentioning

confidence: 99%

Complexes of functionalized quantum dots and chlorin e<sub>6</sub> in photodynamic therapy

Rotomskis¹,

Valančiūnaitė²,

Skripka³

et al. 2013

Lith. J. Phys.

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“…There are in the literature a lot of publications that explore the fundamental interactions between PS and albumins. [107][108][109][110][111][112][113][114] Such studies, which comprise both physicochemical and biophysical insights, represent an extensive field with the general aim of understanding how natural albumins present in the body can, upon injection of bare PS, become PS carriers and deliver them at the target site. However, as the present review deals with biohybrid materials, herein we will focus on a different strategy, consisting of using synthetic hybrids where the albumin is modified with PS prior to biomedical use, in order to enhance their chemical and biological features.…”

Section: Hybrids With Serum Proteinsmentioning

confidence: 99%

Porphyrinoid biohybrid materials as an emerging toolbox for biomedical light management

et al. 2018

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The development of photoactive and biocompatible nanomaterials is a current major challenge of materials science and nanotechnology, as they will contribute to promoting current and future biomedical applications. A growing strategy in this direction consists of using biologically inspired hybrid materials to maintain or even enhance the optical properties of chromophores and fluorophores in biological media. Within this area, porphyrinoids constitute the most important family of organic photosensitizers. The following extensive review will cover their incorporation into different kinds of photosensitizing biohybrid materials, as a fundamental research effort toward the management of light for biomedical use, including technologies such as photochemical internalization (PCI), photoimmunotherapy (PIT), and theranostic combinations of fluorescence imaging and photodynamic therapy (PDT) or photodynamic inactivation (PDI) of microorganisms.

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“…We employed a simple experimental set-up with solutions of talaporfin sodium and albumin to study the interaction. Simple set-ups using a photosensitizer and binding protein are generally used to study the oxidation capability of photosensitization reactions or interactions with proteins [13,14]. Our results suggest that the therapeutic interaction with human serum albumin may be stronger than with bovine serum albumin.…”

Section: Discussionmentioning

confidence: 54%

“…Among serum proteins, low-density lipoprotein has also been widely studied in regards to photodynamic therapeutic interactions [16], because malignant tumors, which are general therapeutic targets of photosensitization reactions, activate low-density lipoprotein receptors. On the other hand, oxidation of bovine serum albumin, which is generally used as a photosensitizer binding protein in vitro, has been studied in regards to its therapeutic interaction and aggregation [14]. However, to the best of our knowledge, there have been no reports comparing the oxidation of human and bovine serum albumin by photosensitization reactions.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of human and bovine serum albumin on oxidation characteristics by a photosensitization reaction under complete binding of talaporfin sodium

Kurotsu

Yajima

Takahashi

et al. 2015

Photodiagnosis and Photodynamic Therapy

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Photoprocesses of chlorin e6 bound to lysozyme or bovin serum albumin

Cited by 14 publications

References 46 publications

Complexes of functionalized quantum dots and chlorin e<sub>6</sub> in photodynamic therapy

Complexes of functionalized quantum dots and chlorin e<sub>6</sub> in photodynamic therapy

Porphyrinoid biohybrid materials as an emerging toolbox for biomedical light management

Evaluation of human and bovine serum albumin on oxidation characteristics by a photosensitization reaction under complete binding of talaporfin sodium

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