scholarly journals A Novel NiFe2O4/Paper-Based Magnetoelastic Biosensor to Detect Human Serum Albumin

Sensors ◽  
2020 ◽  
Vol 20 (18) ◽  
pp. 5286
Author(s):  
Xing Guo ◽  
Rong Liu ◽  
Hongmei Li ◽  
Jingzhe Wang ◽  
Zhongyun Yuan ◽  
...  

For the first time, a novel NiFe2O4/paper-based magnetoelastic (ME) biosensor was developed for rapid, sensitive, and portable detection of human serum albumin (HSA). Due to the uniquely magnetoelastic effect of NiFe2O4 nanoparticles and the excellent mechanical properties of the paper, the paper-based ME biosensor transforms the surface stress signal induced by the specific binding of HSA and antibody modified on the paper into the electromagnetic signal. The accumulated binding complex generates a compressive stress on the biosensor surface, resulting in a decrease in the biosensor’s static magnetic permeability, which correlates to the HSA concentrations. To improve the sensitivity of the biosensor, the concentration of NiFe2O4 nanofluid and the impregnated numbers of the NiFe2O4 nanofluid-impregnated papers were optimized. The experimental results demonstrated that the biosensor exhibited a linear response to HSA concentrations ranging from 10 μg∙mL−1 to 200 μg∙mL−1, with a detection limit of 0.43 μg∙mL−1, which is significantly lower than the minimal diagnosis limit of microalbuminuria. The NiFe2O4/paper-based ME biosensor is easy to fabricate, and allows the rapid, highly-sensitive, and selective detection of HSA, providing a valuable analytical device for early monitoring and clinical diagnosis of microalbuminuria and nephropathy. This study shows the successful integration of the paper-based biosensor and the ME sensing analytical method will be a highly-sensitive, easy-to-use, disposable, and portable alternative for point-of-care monitoring.

2019 ◽  
Vol 55 (97) ◽  
pp. 14574-14577 ◽  
Author(s):  
Soyeon Yoo ◽  
Min Su Han

We report a novel turn-on sensing probe for the detection of butyrylcholinesterase activity in human serum using a fluorophore with high binding affinity for HSA.


1983 ◽  
Vol 64 (3) ◽  
pp. 307-314 ◽  
Author(s):  
M. Jawed Iqbal ◽  
Maureen Dalton ◽  
Robert S. Sawers

1. The percentage binding of testosterone (T) and oestradiol (E2) to sex hormone binding globulin (SHBG) and human serum albumin (HSA) was determined over a range of SHBG concentrations of 16–250 nmol of dihydrotestosterone (DHT) bound/l. It was found that the binding of both T and E2 to HSA was a function of their binding to SHBG and bore an inverse relationship to it. After removal of both SHBG and HSA from plasma by affinity chromatography a ‘residual’ binding of about 11% for T and 12% for E2 was still apparent. in addition to the specific high-affinity, low capacity binding of E2 to SHBG, non-specific low-affinity binding of 7–12% was demonstrated after selective denaturation of the specific binding site of the latter. 2. Competition studies indicated that although at the relatively higher levels of SHBG found in the normal female the physiological concentrations of E2, T and DHT need not be taken into account in estimating the unbound fractions of steroids, at the relatively lower levels of SHBG found in normal men and hirsute women, the physiological concentrations of T and DHT are effective in causing statistically significant displacement of E2 from the common, specific binding site on SHBG. 3. A simple computerized technique is described for the determination of fractions of E2 and T respectively, that are unbound to SHBG, unbound to SHBG and HSA, and unbound to all plasma proteins, when the total plasma levels of E2, T, DHT and SHBG are known.


2011 ◽  
Vol 39 (3) ◽  
pp. 2781-2787 ◽  
Author(s):  
Yan-Jun Hu ◽  
Chao-Hui Chen ◽  
Shu Zhou ◽  
Ai-Min Bai ◽  
Yu Ou-Yang

2020 ◽  
Vol 132 (8) ◽  
pp. 3155-3160
Author(s):  
Zijie Luo ◽  
Taoyuze Lv ◽  
Kangning Zhu ◽  
Yi Li ◽  
Lei Wang ◽  
...  

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