Abstract
Background: In order to investigate the therapeutic interaction of an extra-cellular photosensitization reaction, we evaluated the oxidation characteristics of human and bovine serum albumin by this reaction with talaporfin sodium under complete binding with albumin by spectroscopic analysis in a cell-free solution. Methods: The solution was composed of 20. μg/ml talaporfin sodium and 2.1. mg/ml human or bovine serum albumin. A 662. nm laser light was used to irradiate the solution. Visible absorbance spectra of solutions were measured to obtain the oxidized and non-oxidized relative densities of albumin and talaporfin sodium before and after the photosensitization reaction. The defined oxidation path ratio of talaporfin sodium to albumin reflected the oxidation of the solution. Absorbance wavelengths at approximately 240 and 660. nm were used to calculate normalized molecular densities of oxidized albumin and talaporfin sodium, respectively. Results and conclusions: The oxidation path ratio of talaporfin sodium to albumin when binding human serum albumin was approximately 1.8 times larger than that of bovine serum albumin during the photosensitization reaction from 1 to 50J/cm<sup>2</sup>. We hypothesized that the oxidation path ratio results might have been caused by talaporfin sodium binding affinity or binding location difference between the two albumins, because the fluorescence lifetimes of talaporfin sodium bound to human and bovine serum albumin were 7.0 and 4.9ns, respectively. Therefore, the photodynamic therapeutic interaction might be stronger with human serum albumin than with bovine serum albumin in the case of extracellular photosensitization reaction.
| Original language | English |
|---|---|
| Pages (from-to) | 408-413 |
| Number of pages | 6 |
| Journal | Photodiagnosis and Photodynamic Therapy |
| Volume | 12 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2015 Sep 1 |
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Keywords
- Bovine serum albumin
- Extra-cellular photosensitization reaction
- Human serum albumin
- Oxidation characteristics
- Talaporfin sodium
- Therapeutic interaction
ASJC Scopus subject areas
- Biophysics
- Oncology
- Dermatology
- Pharmacology (medical)
Cite this
Evaluation of human and bovine serum albumin on oxidation characteristics by a photosensitization reaction under complete binding of talaporfin sodium. / Kurotsu, Mariko; Yajima, Masahiro; Takahashi, Mei; Ogawa, Emiyu; Arai, Tsunenori.
In: Photodiagnosis and Photodynamic Therapy, Vol. 12, No. 3, 01.09.2015, p. 408-413.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Evaluation of human and bovine serum albumin on oxidation characteristics by a photosensitization reaction under complete binding of talaporfin sodium
AU - Kurotsu, Mariko
AU - Yajima, Masahiro
AU - Takahashi, Mei
AU - Ogawa, Emiyu
AU - Arai, Tsunenori
PY - 2015/9/1
Y1 - 2015/9/1
N2 - Background: In order to investigate the therapeutic interaction of an extra-cellular photosensitization reaction, we evaluated the oxidation characteristics of human and bovine serum albumin by this reaction with talaporfin sodium under complete binding with albumin by spectroscopic analysis in a cell-free solution. Methods: The solution was composed of 20. μg/ml talaporfin sodium and 2.1. mg/ml human or bovine serum albumin. A 662. nm laser light was used to irradiate the solution. Visible absorbance spectra of solutions were measured to obtain the oxidized and non-oxidized relative densities of albumin and talaporfin sodium before and after the photosensitization reaction. The defined oxidation path ratio of talaporfin sodium to albumin reflected the oxidation of the solution. Absorbance wavelengths at approximately 240 and 660. nm were used to calculate normalized molecular densities of oxidized albumin and talaporfin sodium, respectively. Results and conclusions: The oxidation path ratio of talaporfin sodium to albumin when binding human serum albumin was approximately 1.8 times larger than that of bovine serum albumin during the photosensitization reaction from 1 to 50J/cm2. We hypothesized that the oxidation path ratio results might have been caused by talaporfin sodium binding affinity or binding location difference between the two albumins, because the fluorescence lifetimes of talaporfin sodium bound to human and bovine serum albumin were 7.0 and 4.9ns, respectively. Therefore, the photodynamic therapeutic interaction might be stronger with human serum albumin than with bovine serum albumin in the case of extracellular photosensitization reaction.
AB - Background: In order to investigate the therapeutic interaction of an extra-cellular photosensitization reaction, we evaluated the oxidation characteristics of human and bovine serum albumin by this reaction with talaporfin sodium under complete binding with albumin by spectroscopic analysis in a cell-free solution. Methods: The solution was composed of 20. μg/ml talaporfin sodium and 2.1. mg/ml human or bovine serum albumin. A 662. nm laser light was used to irradiate the solution. Visible absorbance spectra of solutions were measured to obtain the oxidized and non-oxidized relative densities of albumin and talaporfin sodium before and after the photosensitization reaction. The defined oxidation path ratio of talaporfin sodium to albumin reflected the oxidation of the solution. Absorbance wavelengths at approximately 240 and 660. nm were used to calculate normalized molecular densities of oxidized albumin and talaporfin sodium, respectively. Results and conclusions: The oxidation path ratio of talaporfin sodium to albumin when binding human serum albumin was approximately 1.8 times larger than that of bovine serum albumin during the photosensitization reaction from 1 to 50J/cm2. We hypothesized that the oxidation path ratio results might have been caused by talaporfin sodium binding affinity or binding location difference between the two albumins, because the fluorescence lifetimes of talaporfin sodium bound to human and bovine serum albumin were 7.0 and 4.9ns, respectively. Therefore, the photodynamic therapeutic interaction might be stronger with human serum albumin than with bovine serum albumin in the case of extracellular photosensitization reaction.
KW - Bovine serum albumin
KW - Extra-cellular photosensitization reaction
KW - Human serum albumin
KW - Oxidation characteristics
KW - Talaporfin sodium
KW - Therapeutic interaction
UR - http://www.scopus.com/inward/record.url?scp=84940901175&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84940901175&partnerID=8YFLogxK
U2 - 10.1016/j.pdpdt.2015.05.008
DO - 10.1016/j.pdpdt.2015.05.008
M3 - Article
C2 - 26072295
AN - SCOPUS:84940901175
VL - 12
SP - 408
EP - 413
JO - Photodiagnosis and Photodynamic Therapy
JF - Photodiagnosis and Photodynamic Therapy
SN - 1572-1000
IS - 3
ER -