scholarly journals Demonstration of specific binding sites for human serum albumin in group C and G streptococci.

1980 ◽  
Vol 27 (1) ◽  
pp. 6-14 ◽  
Author(s):  
E B Myhre ◽  
G Kronvall
Talanta ◽  
2004 ◽  
Vol 63 (2) ◽  
pp. 503-508 ◽  
Author(s):  
C. André ◽  
Y.C. Guillaume

2012 ◽  
Vol 18 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Orsolya Dömötör ◽  
Christian G. Hartinger ◽  
Anna K. Bytzek ◽  
Tamás Kiss ◽  
Bernhard K. Keppler ◽  
...  

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.


2013 ◽  
Vol 104 (2) ◽  
pp. 430a ◽  
Author(s):  
Eileen S. Krenzel ◽  
Heidi A. Schwanz ◽  
Ravi Jasu ◽  
Michael Zakharov ◽  
Shalendar Bhasin ◽  
...  

2020 ◽  
Vol 21 (16) ◽  
pp. 5740
Author(s):  
Hrvoje Rimac ◽  
Tana Tandarić ◽  
Robert Vianello ◽  
Mirza Bojić

Human serum albumin (HSA) is the most abundant carrier protein in the human body. Competition for the same binding site between different ligands can lead to an increased active concentration or a faster elimination of one or both ligands. Indomethacin and quercetin both bind to the binding site located in the IIA subdomain. To determine the nature of the HSA-indomethacin-quercetin interactions, spectrofluorometric, docking, molecular dynamics studies, and quantum chemical calculations were performed. The results show that the indomethacin and quercetin binding sites do not overlap. Moreover, the presence of quercetin does not influence the binding constant and position of indomethacin in the pocket. However, binding of quercetin is much more favorable in the presence of indomethacin, with its position and interactions with HSA significantly changed. These results provide a new insight into drug-drug interactions, which can be important in situations when displacement from HSA or other proteins is undesirable or even desirable. This principle could also be used to deliberately prolong or shorten the xenobiotics’ half-life in the body, depending on the desired outcomes.


2019 ◽  
Vol 17 (1) ◽  
pp. 806-812
Author(s):  
Liangliang Liu ◽  
Yi Liu ◽  
Aiping Xiao ◽  
Shiyong Mei ◽  
Yixi Xie

AbstractIncreasing the degree of glycation in diabetes could affect the ability of plasma proteins in binding to small molecules and active compounds. In this study, the influence of glycation of Human serum albumin (HSA) on the binding affinities for six dietary flavonoids was investigated by fluorescence spectra. Glycated HSA was prepared through incubation with glucose and characterized by several methods to confirm the glycation. It was found that the level of glycation increased with the increasing incubation time. The glycation of HSA increased the binding affinities for flavonoids by 1.40 to 48.42 times, which indicates that modifications caused by the glycation may have different influences on the interactions of flavonoids with HSA at separate binding sites on this protein. These results are valuable for understanding the influence of diabetes on the metabolism of flavonoids and other bioactive small molecules in human body.


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.


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