| Literature DB >> 31549191 |
Pablo J Gonçalves1,2, Fabio C Bezerra3, Luciane M Almeida4, Lais Alonso3, Guilherme R L Souza5, Antonio Alonso3, Sergio C Zílio3,6, Iouri E Borissevitch3,7.
Abstract
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.Entities:
Keywords: Interaction with albumin; Porphyrin photophysical characteristics; TSPP4 porphyrin; Z-scan
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Year: 2019 PMID： 31549191 DOI： 10.1007/s00249-019-01397-w
Source DB: PubMed Journal: Eur Biophys J ISSN： 0175-7571 Impact factor: 1.733