Comparison of human serum and bovine serum albumins on oxidation dynamics induced by talaporfin sodium photosensitization reaction with albumin rich conditions

Solution experiments

Mariko Kurotsu, Tetsuya Nakamura, Mei Takahashi, Emiyu Ogawa, Tsunenori Arai

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Citation (Scopus)

Abstract

In order to understand extracellular-photosensitization reaction (PR) using talaporfin sodium, we studied comparison of oxidation dynamics of albumin and talaporfin sodium in solution system by visible and ultraviolet absorption spectrum measurements. Almost all talaporfin sodium particles may be bound to albumin in interstitial fluid, and this binding would affect the oxidation dynamics during this PR. Bovine serum albumin (BSA) is commonly used in vitro study but its binding characteristics with talaporfin sodium are different from human serum albumin (HSA). PR was operated in a solution composed of 20 μg/ml talaporfin sodium and 1.3 mg/ml HSA or BSA to simulate myocardial extracellular PR condition. Laser radiation of 662 nm was irradiated to this solution with irradiance of 0.29 W/cm2. Absorption spectra of these solutions were measured during the PR. We estimated oxidized ratio by absorption difference around 240 nm before and after the PR. Talaporfin sodium was oxidized 100% with HSA and BSA by the PR of 100 J/cm2 in radiant exposure. On the other hand, HSA and BSA were oxidized 60% and 94%, respectively in this radiant exposure. Q-band absorption peak of talaporfin sodium with HSA was shifted to 1 nm longer wavelength increasing radiant exposure up to 100 J/cm2. This longer wavelength shift would mean binding ratio of non-oxidized talaporfin sodium to non-oxidized HSA was increased with increasing radiant exposure. Therefore it would be possible that PR with talaporfin sodium bound to HSA might present efficient PDT than PR bound to BSA.

Original languageEnglish
Title of host publicationProgress in Biomedical Optics and Imaging - Proceedings of SPIE
PublisherSPIE
Volume8941
ISBN (Print)9780819498540
DOIs
Publication statusPublished - 2014
EventOptical Interactions with Tissue and Cells XXV; and Terahertz for Biomedical Applications - San Francisco, CA, United States
Duration: 2014 Feb 22014 Feb 4

Other

OtherOptical Interactions with Tissue and Cells XXV; and Terahertz for Biomedical Applications
CountryUnited States
CitySan Francisco, CA
Period14/2/214/2/4

Fingerprint

Photosensitivity Disorders
Bovine Serum Albumin
albumins
serums
Albumins
Serum Albumin
Sodium
sodium
Oxidation
oxidation
Serum
Experiments
Absorption spectra
Talaporfin
absorption spectra
Wavelength
Extracellular Fluid
Laser radiation
Lasers
ultraviolet absorption

Keywords

  • Absorbance
  • Extracellular interstitial space
  • Oxidized ratio
  • UV-Vis spectrum

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics
  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Radiology Nuclear Medicine and imaging

Cite this

Kurotsu, M., Nakamura, T., Takahashi, M., Ogawa, E., & Arai, T. (2014). Comparison of human serum and bovine serum albumins on oxidation dynamics induced by talaporfin sodium photosensitization reaction with albumin rich conditions: Solution experiments. In Progress in Biomedical Optics and Imaging - Proceedings of SPIE (Vol. 8941). [89410F] SPIE. https://doi.org/10.1117/12.2039028

Comparison of human serum and bovine serum albumins on oxidation dynamics induced by talaporfin sodium photosensitization reaction with albumin rich conditions : Solution experiments. / Kurotsu, Mariko; Nakamura, Tetsuya; Takahashi, Mei; Ogawa, Emiyu; Arai, Tsunenori.

Progress in Biomedical Optics and Imaging - Proceedings of SPIE. Vol. 8941 SPIE, 2014. 89410F.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Kurotsu, M, Nakamura, T, Takahashi, M, Ogawa, E & Arai, T 2014, Comparison of human serum and bovine serum albumins on oxidation dynamics induced by talaporfin sodium photosensitization reaction with albumin rich conditions: Solution experiments. in Progress in Biomedical Optics and Imaging - Proceedings of SPIE. vol. 8941, 89410F, SPIE, Optical Interactions with Tissue and Cells XXV; and Terahertz for Biomedical Applications, San Francisco, CA, United States, 14/2/2. https://doi.org/10.1117/12.2039028
Kurotsu M, Nakamura T, Takahashi M, Ogawa E, Arai T. Comparison of human serum and bovine serum albumins on oxidation dynamics induced by talaporfin sodium photosensitization reaction with albumin rich conditions: Solution experiments. In Progress in Biomedical Optics and Imaging - Proceedings of SPIE. Vol. 8941. SPIE. 2014. 89410F https://doi.org/10.1117/12.2039028
Kurotsu, Mariko ; Nakamura, Tetsuya ; Takahashi, Mei ; Ogawa, Emiyu ; Arai, Tsunenori. / Comparison of human serum and bovine serum albumins on oxidation dynamics induced by talaporfin sodium photosensitization reaction with albumin rich conditions : Solution experiments. Progress in Biomedical Optics and Imaging - Proceedings of SPIE. Vol. 8941 SPIE, 2014.
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abstract = "In order to understand extracellular-photosensitization reaction (PR) using talaporfin sodium, we studied comparison of oxidation dynamics of albumin and talaporfin sodium in solution system by visible and ultraviolet absorption spectrum measurements. Almost all talaporfin sodium particles may be bound to albumin in interstitial fluid, and this binding would affect the oxidation dynamics during this PR. Bovine serum albumin (BSA) is commonly used in vitro study but its binding characteristics with talaporfin sodium are different from human serum albumin (HSA). PR was operated in a solution composed of 20 μg/ml talaporfin sodium and 1.3 mg/ml HSA or BSA to simulate myocardial extracellular PR condition. Laser radiation of 662 nm was irradiated to this solution with irradiance of 0.29 W/cm2. Absorption spectra of these solutions were measured during the PR. We estimated oxidized ratio by absorption difference around 240 nm before and after the PR. Talaporfin sodium was oxidized 100{\%} with HSA and BSA by the PR of 100 J/cm2 in radiant exposure. On the other hand, HSA and BSA were oxidized 60{\%} and 94{\%}, respectively in this radiant exposure. Q-band absorption peak of talaporfin sodium with HSA was shifted to 1 nm longer wavelength increasing radiant exposure up to 100 J/cm2. This longer wavelength shift would mean binding ratio of non-oxidized talaporfin sodium to non-oxidized HSA was increased with increasing radiant exposure. Therefore it would be possible that PR with talaporfin sodium bound to HSA might present efficient PDT than PR bound to BSA.",
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