A fluorescent probe for butyrylcholinesterase activity in human serum based on a fluorophore with specific binding affinity for human serum albumin

2019 ◽  
Vol 55 (97) ◽  
pp. 14574-14577 ◽  
Author(s):  
Soyeon Yoo ◽  
Min Su Han
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescent Probe ◽  
Binding Affinity ◽  
Specific Binding ◽  
Turn On ◽  
High Binding ◽  
Butyrylcholinesterase Activity ◽  
High Binding Affinity

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.

Interaction of the 5-fluorouracil analog 5-fluoro-2′-deoxyuridine with ‘N’ and ‘B’ isoforms of human serum albumin: a spectroscopic and calorimetric study

2014 ◽  
Vol 10 (11) ◽  
pp. 2954-2964 ◽  
Author(s):  
Mohd Ishtikhar ◽  
Shawez Khan ◽  
Gamal Badr ◽  
Amany Osama Mohamed ◽  
Rizwan Hasan Khan
Keyword(s):  
Thermal Stability ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity ◽  
Calorimetric Study ◽  
High Binding ◽  
High Binding Affinity

5-Fluoro-2′-deoxyuridine, an analog of 5-fluorouracil, has high binding affinity and thermal stability toward the N-isoform compared to the B-isoform of HSA.

Competition Binding Experiments for Rapidly Ranking Lead Molecules for their Binding Affinity to Human Serum Albumin

2002 ◽  
Vol 5 (8) ◽  
pp. 645-650 ◽  
Author(s):  
Chaohong Claudio Dalvita ◽  
Maria Flocco ◽  
Brian J. Stockman ◽  
Marina Veronesi
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity ◽  
Competition Binding

Interaction between a novel intramolecular charge transfer fluorescent probe PFEP and human serum albumin

2010 ◽  
Vol 21 (4) ◽  
pp. 480-483 ◽  
Author(s):  
Dong Ju ◽  
Sheng Mei Song ◽  
Yan Bo Wu ◽  
Shao Min Shuang ◽  
Chuan Dong
Keyword(s):  
Charge Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescent Probe ◽  
Intramolecular Charge Transfer

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 ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Specific Binding ◽  
Point Of Care ◽  
Electromagnetic Signal ◽  
Portable Detection ◽  
Highly Sensitive ◽  
Stress Signal ◽  
Nife2o4 Nanoparticles

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.

Exploring the potential of a urea derivative: an AIE-luminogen and its interaction with human serum albumin in aqueous medium

The Analyst ◽  
2019 ◽  
Vol 144 (8) ◽  
pp. 2696-2703 ◽  
Author(s):  
Senjuti Halder ◽  
Soham Samanta ◽  
Gopal Das
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Aqueous Medium ◽  
Urea Derivative ◽  
Urea Molecule ◽  
Fluorescence Response ◽  
Turn On

A simple AIE active urea molecule (L1) can selectively interact with HSAviaturn-on fluorescence response in aqueous medium.

The binding affinity of amino acid–protein: hydroxyproline binding site I on human serum albumin

2012 ◽  
Vol 10 (41) ◽  
pp. 8314 ◽  
Author(s):  
Ximin Zhou ◽  
Wenjuan Lü ◽  
Li Su ◽  
Yalei Dong ◽  
Qianfeng Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Affinity ◽  
Acid Protein ◽  
Amino Acid Protein
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