Molecular engineering of a fluorescent probe for highly efficient detection of human serum albumin in biological fluid

Human serum albumin (HSA) is synthesized by the liver, accounting for 60 % of total plasma protein in vertebrates' blood. It is the most predominant extracellular plasma protein that acts as a repository and transporter of exogenous and endogenous substances in the blood of healthy humans. Decr...

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Veröffentlicht in:Sensors international 2025, Vol.6, p.100304, Article 100304
Hauptverfasser: Chinnappan, Raja, Mir, Tanveer Ahmad, Easwaramoorthi, Shanmugam, Sunil, Gopika, Feba, Ancy, Kanagasabai, Balamurugan, Wani, Shadil Ibrahim, Sandouka, Maram N., Alzhrani, Alaa, Devanesan, Sandhanasamy, AlSalhi, Mohamad S., Mani, Naresh Kumar, Al-Kattan, Wael, Yaqinuddin, Ahmed, Assiri, Abdullah M., Broering, Dieter C.
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Sprache:eng
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Zusammenfassung:Human serum albumin (HSA) is synthesized by the liver, accounting for 60 % of total plasma protein in vertebrates' blood. It is the most predominant extracellular plasma protein that acts as a repository and transporter of exogenous and endogenous substances in the blood of healthy humans. Decreased albumin concentration in the human body or its abnormal levels indicate the occurrence of hepatic, renal, and digestive-related diseases. Therefore, accurate quantification of HSA is of great significance in diagnostic testing and routine clinical analysis of albumin-linked diseases. Herein, a class of triphenylamine rhodanine-3-acetic acid (mRA)-a bifunctional fluorescent molecule with twisted intramolecular charge transfer (TICT)-induced emission characteristics is synthesized and employed as a novel sensing probe for the fluorescent detection of human albumin. mRA can be selectively lighted up through site-specific interactions with serum albumin-binding moieties and show enhanced photophysical or biological response efficacy. Understanding the interaction of mRA with HSA at the molecular level was carried out using docking methodology to explore the site-specific interaction phenomenon. The resulting fluorescence strategy produced a dose-dependent signal response enhancement upon interaction with HSA in the concentration range of 0.01–400 μg/ml. The sensor probe exhibits a low detection limit of 10 ng/mL and is found to be a feasible, low-cost, and effective approach for HSA analysis in complex biological fluids for early detection and diagnosis of albumin-related diseases. Human serum albumin (HSA) levels in plasma are one of the important indicators of liver function. HSA-induced Turn-on fluorescence emission of Triphenylamine rhodanine-3-acetic acid (mRA) exploited for the quantitative detection of HSA. The affinity and selective binding of mRA with HSA have been demonstrated. [Display omitted] •A simple fluorescence-based quantitative detection of Human serum albumin has been demonstrated•Triphenylamine rhodanine-3-acetic acid (mRA)- with twisted intramolecular charge transfer (TICT)- employed as a novel sensing probe•A fifty-fold enhancement in the fluorescence of the probe dye by HSA facilitates the low limit of detection•The probe dye has high affinity and specificity for HSA without any cross-reactivity of other closely associated biomolecules.•This method has been used for the analysis of the biological fluid derived from liver cancer cell supernat
ISSN:2666-3511
2666-3511
DOI:10.1016/j.sintl.2024.100304