Dual luminescent charge transfer probe for quantitative detection of serum albumin in aqueous samples

Choudhury, Rajib; Quattlebaum, Benjamin; Conkin, Charles; Patel, Siddhi Rajeshbhai; Mendenhall, Kallie

doi:10.1016/j.saa.2020.118305

Cited by 9 publications

(4 citation statements)

References 36 publications

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“…The stoichiometric ratio of the complex formed by HSA and M–OH–SO 3 was measured using Job’s plot analysis, which indicated that M–OH–SO 3 and HSA mainly formed a 1:1 complex (Figure E). , It is known that HSA possesses different binding sites, of which the main binding sites are located in the hydrophobic cavity of IIA and IIIA subdomains. − To explore the potential binding sites of HSA for M–OH–SO 3 , three drug inhibitors were utilized (warfarin, domain IIA marker; salicylic acid, subdomain IB and IIA site markers; and ibuprofen, site IIIA marker) through a competitive binding assay . The fluorescence intensity changes suggested that M–OH–SO 3 binds to the three sites IIA and IIIA of HSA (Figure F).…”

Section: Resultsmentioning

confidence: 99%

“…37−39 To explore the potential binding sites of HSA for M−OH−SO 3 , three drug inhibitors were utilized (warfarin, domain IIA marker; salicylic acid, subdomain IB and IIA site markers; and ibuprofen, site IIIA marker) through a competitive binding assay. 40 The fluorescence intensity changes suggested that M−OH−SO 3 binds to the three sites IIA and IIIA of HSA (Figure 1F).…”

Section: ■ Experimental Sectionmentioning

confidence: 97%

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Dual-Channel Recognition of Human Serum Albumin and Glutathione by Fluorescent Probes with Site-Dependent Responsive Features

Yuan

Pan

et al. 2022

Anal. Chem.

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Design of chemical probes with high specificity and responses are particularly intriguing. In this work, a fluorescent probe (M–OH–SO 3 ) with dual-channel spectral responses toward human serum albumin (HSA) is presented. By employing dinitrobenzenesulfonate as a recognition site as well as a fluorescence quencher, probe M–OH–SO 3 displayed weak fluorescence, which, nevertheless, exhibits extensive yellow (575 nm) and red (660 nm) fluorescence emissions toward HSA under excitations at 400 and 500 nm, respectively. Interestingly, M–OH–SO 3 displayed the best performance toward HSA with distinctly higher selectivity than that of its counterparts M–SO 3 , M–H–SO 3 , and M–F–SO 3 , which were prepared simply by modulating the functional group at the ortho position of the dicyanoisophorone core. Molecular docking results revealed that M–OH–SO 3 possesses the lowest binding energy among the tested derivatives and accordingly the strongest binding affinity. Probe M–OH–SO 3 showed a good linear relationship toward HSA in a range of 0.5–18 μM with a limit of detection of 35 nM. Cell imaging results demonstrated that probe M–OH–SO 3 could visualize the variation HSA levels in hepatocarcinoma cells. In addition, probe M–OH–SO 3 could also be employed for the recognition of glutathione through the cleavage of the dinitrobenzenesulfonate group along with an enhancement of emission at 575 nm. The site-dependent properties inspired a novel paradigm for design of fluorescent probes with optimized selectivity and responses.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Experimental Sectionmentioning

confidence: 97%

Dual-Channel Recognition of Human Serum Albumin and Glutathione by Fluorescent Probes with Site-Dependent Responsive Features

Yuan

Pan

et al. 2022

Anal. Chem.

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“…Subsequently, they synthesized probe 13 based on the FA1 site, which specifically responded to HSA after deprotonation at physiological pH. 59 It exhibited fluorescence enhancement at 665 and 780 nm with detection limits of 10 and 20 mg/L, respectively.…”

Section: Detection Of Hsa Based On Spatialmentioning

confidence: 99%

“…In 2019, Choudhury et al prepared fluorescent probe 12 with a detection limit as low as 1 mg/L, which could be used to quantitatively determine HSA in clinical urine and blood samples. Subsequently, they synthesized probe 13 based on the FA1 site, which specifically responded to HSA after deprotonation at physiological pH . It exhibited fluorescence enhancement at 665 and 780 nm with detection limits of 10 and 20 mg/L, respectively.…”

Section: Fluorescence Probes For Qualitative and Quantitative Hsamentioning

confidence: 99%

Development of Human Serum Albumin Fluorescent Probes in Detection, Imaging, and Disease Therapy

Wang,

Huo,

Yin

2024

J. Phys. Chem. B

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Human serum albumin (HSA) acts as a repository and transporter of substances in the blood. An abnormal concentration may indicate the occurrence of liver-and kidney-related diseases, which has attracted people to investigate the precise quantification of HSA in body fluids. Fluorescent probes can combine with HSA covalently or noncovalently to quantify HSA in urine and plasma. Moreover, probes combined with HSA can improve its photophysical properties; probe-HSA has been applied in real-time monitoring and photothermal and photodynamic therapy in vivo. This Review will introduce fluorescent probes for quantitative HSA according to the three reaction mechanisms of spatial structure, enzymatic reaction, and self-assembly and systematically introduce the application of probes combined with HSA in disease imaging and phototherapy. It will help develop multifunctional applications for HSA probes and provide assistance in the early diagnosis and treatment of diseases.

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HSA over BSA: Selective detection of Human Serum Albumin via a naphtho [2,1‐b] furan‐based system

Bandyopadhyay,

Hazra,

Roy

et al. 2024

Chemistry An Asian Journal

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Human serum albumin (HSA) is an important biomarker that can be used for the early diagnosis of many diseases. In this work, a TICT probe bearing fused naphtho‐furan scaffold (NPNF) was developed and employed in the selective turn‐on sensing of HSA. The probe’s selectivity towards HSA was observed using steady‐state fluorescence experiments, with limit of quantitation in micromolar levels. NPNF also displayed its capability exclusively towards HSA over bovine serum albumin (BSA), which was studied/rationalized using anisotropy and time‐resolved studies. Molecular docking was used to shed light on the location of NPNF in the domain I of HSA. The practical application of the probe was also demonstrated by the detection of HSA in urine and the HSA‐assisted detection of cerium.

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Dual luminescent charge transfer probe for quantitative detection of serum albumin in aqueous samples

Cited by 9 publications

References 36 publications

Dual-Channel Recognition of Human Serum Albumin and Glutathione by Fluorescent Probes with Site-Dependent Responsive Features

Dual-Channel Recognition of Human Serum Albumin and Glutathione by Fluorescent Probes with Site-Dependent Responsive Features

Development of Human Serum Albumin Fluorescent Probes in Detection, Imaging, and Disease Therapy

HSA over BSA: Selective detection of Human Serum Albumin via a naphtho [2,1‐b] furan‐based system

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