Mohd Khairuddin Md Arshad
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Preferred name
Mohd Khairuddin Md Arshad
Official Name
Mohd Khairuddin , Md Arshad
Alternative Name
Md. Arshad, M. K.
Arshad, Mohd K.M.
Arshad, M. K.M.
Khairuddin Md Arshad, Mohd
Arshad, M. K.Md
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Scopus Author ID
57211870224
Researcher ID
L-5830-2013

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  • Publication
    Selective detection of amyloid fibrils by a dipole moment mechanism on dielectrode – Structural insights by in silico analysis
    ( 2023-03-01)
    Adam H.
    ;
    Subash Chandra Bose Gopinath
    ;
    Kumarevel T.
    ;
    Mohd Khairuddin Md Arshad
    ;
    Adam T.
    ;
    Zaliman Sauli
    ;
    Subramaniam S.
    ;
    Uda Hashim
    ;
    Chen Y.
    Amyloid fibrils are associated with different neurodegenerative diseases, a final product of several protein aggregation pathways. Parkinson's disease is a type of amyloidosis, characterized by the accumulation and propagation of amyloid fibrils of alpha-synuclein. The detection of fibrils at low concentrations is critical for the diagnosis of Parkinson's disease. We report a novel technique for the selective detection of amyloid fibrils through a dipole moment on a dielectrode surface. A sensitive dielectrode sensor for detecting aggregation of alpha synuclein and works by interacting an antibody on two-electrode surface functionalized gold interdigitated electrode. For the physical characterization of the sensing surface and finger electrodes, high-power microscope, scanning electron microscope, and 3D-profilormeter were used. Electrical characterization was performed on the sensing surface by using Keithley 6487 picoammeter. Based on the stability analysis with various electrolytes solutions, the sensor was found to be stable from pH 3. Further, under optimal circumstances, a linear range of alpha synuclein fibril detection was from 100 aM to 100 pM [y = 5E-06x + 5E-06; R² = 0.9724], and the limit of detection was estimated to be 100 aM based on S/N = 3. This study was further anchored by molecular docking analysis with synuclein peptide (47−56). We predict that advancements in this direction will assist in clarifying the complex process posed by Parkinson's disease.
      2
  • Publication
    Distinguishing normal and aggregated alpha-synuclein interaction on gold nanorod incorporated zinc oxide nanocomposite by electrochemical technique
    ( 2021-02-28)
    Adam H.
    ;
    Subash Chandra Bose Gopinath
    ;
    Mohd Khairuddin Md Arshad
    ;
    Nor Azizah Parmin
    ;
    Uda Hashim
    Misfolding and accumulation of the protein alpha synuclein in the brain cells characterize Parkinson's disease (PD). Electrochemical based aluminum interdigitated electrodes (ALIDEs) was fabricated by using conventional photolithography method and modified the surfaces with zinc oxide and gold nanorod by using spin coating method for the analysis of PD protein biomarker. The device surface modified with gold nanorod of 25 nm diameter was used. The bare devices and the surface modified devices were characterized by Scanning Electron Microscope, 3D-Profilometer, Atomic Force Microscope and high-power microscope. The above measurement was also performed to measure the interaction of antibody with aggregated alpha-synuclein for normal, aggregated and aggregated alpha synuclein in human serum and distinguished against 3 control proteins (PARK1, DJ-1 and Factor IX). The detection limit for normal alpha synuclein was 1 f. with the sensitivity of 1 f. on a linear regression (R2 = 0.9759). The detection limit for aggregated alpha synuclein was 10 aM with the sensitivity of 1 aM on a linear regression (R2 = 0.9797). Also, the detection limit of aggregated alpha synuclein in serum was 10 aM with the sensitivity of 1 aM on a linear regression (R2 = 0.9739). These results however indicate that, serum has only minimal amount of alpha synuclein.
      35  5
  • Publication
    Aptasensing nucleocapsid protein on nanodiamond assembled gold interdigitated electrodes for impedimetric SARS-CoV-2 infectious disease assessment
    ( 2022-02-01)
    Ramanathan S.
    ;
    Subash Chandra Bose Gopinath
    ;
    Ismail Z.H.
    ;
    Mohd Khairuddin Md Arshad
    ;
    Prabakaran A/L Poopalan
    In an aim of developing portable biosensor for SARS-CoV-2 pandemic, which facilitates the point-of-care aptasensing, a strategy using 10 μm gap-sized gold interdigitated electrode (AuIDE) is presented. The silane-modified AuIDE surface was deposited with ∼20 nm diamond and enhanced the detection of SARS-CoV-2 nucleocapsid protein (NCP). The characteristics of chemically modified diamond were evidenced by structural analyses, revealing the cubic crystalline nature at (220) and (111) planes as observed by XRD. XPS analysis denotes a strong interaction of carbon element, composed ∼95% as seen in EDS analysis. The C–C, C[dbnd]C, C[dbnd]O, C[dbnd]N functional groups were well-refuted from XPS spectra of carbon and oxygen elements in diamond. The interrelation between elements through FTIR analysis indicates major intrinsic bondings at 2687-2031 cm−1. The aptasensing was evaluated through electrochemical impedance spectroscopy measurements, using NCP spiked human serum. With a good selectivity the lower detection limit was evidenced as 0.389 fM, at a linear detection range from 1 fM to 100 pM. The stability, and reusability of the aptasensor were demonstrated, showing ∼30% and ∼33% loss of active state, respectively, after ∼11 days. The detection of NCP was evaluated by comparing anti-NCP aptamer and antibody as the bioprobes. The determination coefficients of R2 = 0.9759 and R2 = 0.9772 were obtained for aptamer- and antibody-based sensing, respectively. Moreover, the genuine interaction of NCP aptamer and protein was validated by enzyme linked apta-sorbent assay. The aptasensing strategy proposed with AuIDE/diamond enhanced sensing platform is highly recommended for early diagnosis of SARS-CoV-2 infection.
      1  33