Rashida Akter

Amplified electrochemical detection of a cancer biomarker by enhanced precipitation using horseradish peroxidase attached on carbon nanotubes.

An electrochemical nanoimmunosensor based on multiwall carbon nanotubes (MWCNTs)/gold nanoparticles (AuNPs) was developed for the amplified detection of prostate specific antigen (PSA). The amplified detection was achieved by the enhanced precipitation of 4-chloro-1-naphthol (CN) using a higher number of horseradish peroxidase (HRP) molecules attached on MWCNTs. The PSA nanoimmunosensor was fabricated by immobilizing a monoclonal anti-PSA antibody (anti-PSA) on the AuNP-attached thiolated MWCNT on a gold electrode. The sensor surface was characterized using scanning electron microscope, transmission electron microscope, quartz crystal microbalance, and electrochemical techniques. Cyclic and square wave voltammetric techniques were used to monitor the enhanced precipitation of CN that accumulated on the electrode surface and subsequent decrement in the electrode surface area by monitoring the reduction process of the Fe(CN)(6)(3-)/Fe(CN)(6)(4-) redox couple. Under the optimized experimental condition, the linear range and the detection limit of PSA immunosensor were determined to be 1.0 pg/mL to 10.0 ng/mL and 0.40 ± 0.03 pg/mL, respectively. The validity of the proposed method was compared with an enzyme-linked immunosorbent assay method in various PSA spiked human serum samples.

Increased Electrocatalyzed Performance through Dendrimer-Encapsulated Gold Nanoparticles and Carbon Nanotube-Assisted Multiple Bienzymatic Labels: Highly Sensitive Electrochemical Immunosensor for Protein Detection

A highly sensitive electrochemical carcinoembryonic antigen (CEA) immunosensor was fabricated by covalently immobilizing a monoclonal CEA antibody (anti-CEA, Ab(1)) and a mediator (thionine, Th) on a gold nanoparticle (AuNP)-encapsulated dendrimer (Den/AuNP). Multiwalled carbon nanotube (MWCNT)-supported secondary antibody (Ab(2))-conjugated multiple bienzymes, glucose oxidase (GOx), and horseradish peroxidase (HRP) (Ab(2)/MWCNT/GOx/HRP) were used as electrochemical labels. The highly sensitive detection was achieved by the increased HRP-electrocatalyzed reduction of hydrogen peroxide, which was locally generated by the enzyme GOx. The immunosensor surface was characterized using electrochemical impedance spectroscopy, atomic force microscopy, and quartz crystal microbalance techniques. The Den/AuNP and Ab(2)/MWCNT/GOx/HRP bioconjugates were characterized using high-resolution transmission electron microscopy, scanning electron microscopy, and X-ray photoelectron spectroscopy. Cyclic voltammetry and square wave voltammetry techniques were used to monitor the increased electrocatalyzed reduction of hydrogen peroxide by HRP. The linear dynamic range and the detection limit were determined to be 10.0 pg/mL to 50.0 ng/mL and 4.4 ± 0.1 pg/mL, respectively. The validity of the immunosensor response was tested in various CEA-spiked human serum samples, and the results were compared to those of an enzyme-linked immunosorbent assay method.

Ultrasensitive Nanoimmunosensor by coupling non-covalent functionalized graphene oxide platform and numerous ferritin labels on carbon nanotubes.

An ultrasensitive electrochemical nanostructured immunosensor for a breast cancer biomarker carbohydrate antigen 15-3 (CA 15-3) was fabricated using non-covalent functionalized graphene oxides (GO/Py-COOH) as sensor probe and multiwalled carbon nanotube (MWCNTs)-supported numerous ferritin as labels. The immunosensor was constructed by immobilizing a monoclonal anti-CA 15-3 antibody on the GO modified cysteamine (Cys) self-assembled monolayer (SAM) on an Au electrode (Au/Cys) through the amide bond formation between the carboxylic acid groups of GO/Py-COOH and amine groups of anti-CA 15-3. Secondary antibody conjugated MWCNT-supported ferritin labels (Ab2-MWCNT-Ferritin) were prepared through the amide bond formation between amine groups of Ab2 and ferritin and carboxylic acid groups of MWCNTs. The detection of CA 15-3 was based on the enhanced bioelectrocatalytic reduction of hydrogen peroxide mediated by hydroquinone (HQ) at the GO/Py-COOH-based sensor probe. The GO/Py-COOH-based sensor probe and Ab2-MWCNT-Ferritin labels were characterized using cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS), scanning electron microscope (SEM), transmission electron microscope (TEM), and x-ray photoelectron spectroscopy (XPS) techniques. Using differential pulse voltammetry (DPV) technique, CA 15-3 can be selectively detected as low as 0.01 ± 0.07 U/mL in human serum samples. Additionally, the proposed CA 15-3 immunosensor showed excellent selectivity and better stability in human serum samples, which demonstrated that the proposed immunosensor has potentials in proteomic researches and diagnostics.

A highly sensitive quartz crystal microbalance immunosensor based on magnetic bead-supported bienzymes catalyzed mass enhancement strategy.

A highly sensitive quartz crystal microbalance (QCM) immunosensor based on magnetic bead-supported bienzyme catalyzed mass enhanced strategy was developed for the detection of human immunoglobulin G (hIgG) protein. The high sensitive detection was achieved by increasing the deposited mass on the QCM crystal through the enhanced precipitation of 4-chloro-1-naphthol (CN) using higher amounts of horseradish peroxidase (HRP) and glucose oxidase (GOx) bienzymes attached on the magnetic beads (MB). The protein A (PA) and capture antibody (monoclonal anti-human IgG antibody produced in mouse, Ab1)-based QCM probe and the detection antibody (anti-human IgG antibody produced in goat, Ab2)-based MB/HRP/GOx bienzymatic bioconjugates were characterized using scanning electron microscope, transmission electron microscope, cyclic voltammetry, and electrochemical impedance spectroscopy techniques. Under the optimized experimental condition, the linear range and the detection limit of hIgG immunosensor were determined to be 5.0pg/mL-20.0ng/mL and 5.0±0.18pg/mL, respectively. The applicability of the present hIgG immunosensor was examined in hIgG spiked human serum samples and excellent recoveries of hIgG were obtained.