Abstract
A readily synthesizable fluorescent probe DMAT-π-CAP was evaluated for sensitive and selective detection of human serum albumin (HSA). DMAT-π-CAP showed selective turn-on fluorescence at 730 nm in the presence of HSA with more than 720-fold enhancement in emission intensity ([DMAT-π-CAP] = 10 μM), and rapid detection of HSA was accomplished in 3 s. The fluorescence intensity of DMAT-π-CAP was shown to increase in HSA concentration-dependent manner (Kd = 15.4 ± 3.3 μM), and the limit of detection of DMAT-π-CAP was determined to be 10.9 nM (0.72 mg/L). The 1:1 stoichiometry between DMAT-π-CAP and HSA was determined, and the displacement assay revealed that DMAT-π-CAP competes with hemin for the unique binding site, which rarely accommodates drugs and endogenous compounds. Based on the HSA-selective turn-on NIR fluorescence property as well as the unique binding site, DMAT-π-CAP was anticipated to serve as a fluorescence sensor for quantitative detection of the HSA level in biological samples with minimized background interference. Thus, urine samples were directly analyzed by DMAT-π-CAP to assess albumin levels, and the results were comparable to those obtained from immunoassay. The similar sensitivity and specificity to the immunoassay along with the simple, cost-effective, and fast detection of HSA warrants practical application of the NIR fluorescent albumin sensor, DMAT-π-CAP, in the analysis of albumin levels in various biological environments.
Highlights
Human serum albumin (HSA, 67 kDa) is the liver-produced most abundant protein (0.6 mM)in blood plasma [1]
Hemin share the same binding site in human serum albumin (HSA). These results demonstrate that the specific and hemin same binding site in HSA. These results demonstrate that the binding to theshare heretothe unexplored hemin-binding siteCollectively, of HSA is responsible for the turn-on fluorescence specific binding to the hereto unexplored hemin-binding site of is responsible for the turn-on of DMAT-π-CAP
The fluorescence intensity of DMAT-π-CAP was shown to increase in HSA concentration-dependent manner
Summary
Human serum albumin (HSA, 67 kDa) is the liver-produced most abundant protein (0.6 mM)in blood plasma [1]. Human serum albumin (HSA, 67 kDa) is the liver-produced most abundant protein (0.6 mM). As HSA is synthesized in the liver, hypoalbuminemia is related with liver failure which includes cirrhosis, liver cancer, hepatitis, alcohol-related liver disease, and fatty liver disease [2]. Some people with acute heart failure [3], kidney damage [4], protein-losing nephropathy and enteropathy [5] and malnutrition [6] are susceptible to low albumin levels. Hyperalbuminemia, an increased concentration of albumin in blood, is caused by dehydration and high protein diets [7]. HSA serves as “taxis” for various endogenous compounds by using several ligand binding sites located on the net negatively charged globular surface: HSA binds and transports thyroid hormones, lipid-soluble hormones, unconjugated bilirubin, free fatty acids, and divalent cations Many drugs bind to HSA [9], and this event has great pharmaceutical interest because, upon binding to HSA, both the pharmacokinetic and pharmacodynamic properties of the drugs are affected
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