Effects of bovine serum albumin (BSA) on the excited-state properties of meso-tetrakis(sulfonatophenyl) porphyrin (TPPS4)

被引：14
|
作者：
Goncalves, Pablo J. [1 ,2 ]
Bezerra, Fabio C. [1 ]
Almeida, Luciane M. [3 ]
Alonso, Lais [1 ]
Souza, Guilherme R. L. [4 ]
Alonso, Antonio [1 ]
Zilio, Sergio C. [1 ,5 ]
Borissevitch, Iouri E. [1 ,6 ]
机构：
[1] Univ Fed Goias, Inst Fis, BR-74001970 Goiania, Go, Brazil
[2] Univ Fed Goias, Inst Quim, BR-74001970 Goiania, Go, Brazil
[3] Univ Estadual Goias, Campus Henrique Santillo, BR-75132400 Anapolis, Go, Brazil
[4] Univ Fed Goias, Inst Ciencias Biol, BR-74001970 Goiania, Go, Brazil
[5] Univ Sao Paulo, Inst Fis Sao Carlos, Caixa Postal 369, BR-13560970 Sao Carlos, SP, Brazil
[6] Univ Sao Paulo, FFLCRP, Dept Fis, Av Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP, Brazil
来源：
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2019年 / 48卷 / 08期
关键词：
TSPP4; porphyrin; Interaction with albumin; Porphyrin photophysical characteristics; Z-scan; WATER-SOLUBLE PORPHYRINS; PHOTODYNAMIC THERAPY; FLUORESCENCE; PHTHALOCYANINES; PROTONATION; ABSORPTION; PROTEINS; AGENTS; CELLS; DYE;
D O I：
10.1007/s00249-019-01397-w
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
To infer changes in the photophysical properties of porphyrins due to complexation with albumin, a combination of Z-scan and conventional spectroscopic techniques was employed. We measured the characteristics of excited states of meso-tetrakis(sulfonatophenyl) porphyrin bound to bovine serum albumin and observed that the binding reduces the intersystem crossing quantum yield and increases the internal conversion one. A reverse saturable absorption process was observed in the nanosecond timescale. These results are important for prediction of the efficiency of this complex in medical and optical applications, because associating porphyrins to proteins enables better accumulation in tumors and improves its stability in optical devices, but at the same time, decreases its triplet quantum yield.
引用
收藏
页码：721 / 729
页数：9
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