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