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An albumin structure-dependent fluorescent probe for cell imaging and chemo-photodynamic therapy: an in vitro evaluation

A protein structure-dependent probe (OTB) for human serum albumin (HSA) was designed. Molecular simulation were used to assist probe design. OTB exhibited favorable selective HSA sensitivity and strong HSA binding ability. As a cationic molecule, OTB could form a stable amphipathic complex with wate...

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Published in:Dyes and pigments 2023-12, Vol.220, p.111776, Article 111776
Main Authors: Fan, Jing-Wen, Xu, Shao-Hu, Han, Ying, Yan, Cao-Guo, Wang, Qing
Format: Article
Language:English
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Summary:A protein structure-dependent probe (OTB) for human serum albumin (HSA) was designed. Molecular simulation were used to assist probe design. OTB exhibited favorable selective HSA sensitivity and strong HSA binding ability. As a cationic molecule, OTB could form a stable amphipathic complex with water-soluble pillar [5]arene (WP5). More interestingly, the WP5-OTB complex possessed better HSA responsiveness and stronger HSA binding ability than OTB. The detection limit (3σ/k) of WP5-OTB towards HSA was determined to be 0.33 μM. WP5-OTB complex possessed excellent anti-interference ability in the selective recognition of HSA. Common commercial drugs, fluorescent amino acids, and fatty acids had almost negligible effect on the HSA responsiveness of the complex. The WP5-OTB complex self-assembled into supramolecular fluorescent probe in aqueous solution, and the supramolecular probe possessed favorable HSA-induced bioimaging property, pH-sensitive drug delivery property, and photodynamic activity. [Display omitted] •A cationic ICT probe OTB was designed by fully considering its interaction with HSA.•OTB exhibited favorable serum albumin sensitivity and strong HSA binding ability.•The WP5-OTB complex possessed better HSA responsiveness and binding ability than OTB.•The WP5-OTB complex self-assembled into supramolecular fluorescent probe in solution.•The supramolecular probe had good bioimaging and chemo-photodynamic therapy properties.
ISSN:0143-7208
DOI:10.1016/j.dyepig.2023.111776