Hanna Ilyani Zulhaimi
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Hanna Ilyani Zulhaimi
Official Name
Zulhaimi, Hanna Ilyani
Alternative Name
Zulhaimi, H. I.
Zulhaimi, Hanna Ilyani
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Scopus Author ID
57195980737
Researcher ID
EHU-0262-2022

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Electro-determination of protonation by tungsten anchored carbon nanoparticle on interdigitated gold electrode

2023-12-01 , Hanna Ilyani Zulhaimi , Subash Chandra Bose Gopinath , Farizul Hafiz Kasim , Anbu P.

This study presented an enhanced sensitivity of sensing protons (H+) by anchoring tungsten to carbon nanoparticles (WCN) to encourage high current density on the surface of gold interdigitated electrode (AuIDE). The morphology of the sensor evidences the intactness of electrode surface and suitable for WCN modification. To elucidate the study, unmodified AuIDE was compared to the WCN modified surface. Current-volt analysis was compared with electrolyte scouting in the variation of pH by using a picoammater, which supplied 0.0 to 2.0 V with a 0.1 V ramp interval. It was shown that modified WCN gave the sensitivity in the acidic medium (protons) at the pH 4 with a current density value of 2.5 × 10-5 ampere and increased further with lowering the pH to more acidic. This is due to the fact that the tungsten carbon nanoparticle that is anchored offering more electron density and alters the behavior of the chip. Meanwhile, the current density displayed insignificant changes of current density amplification from pH 5 to 12 with the range of 5.91 × 10-9 to 7.36 × 10-8 Ampere. The deposition of WCN on the AuIDE surface chip revealed the successfulness of this nanoparticle in chemically linked with the AuIDE surface and how modified nanoparticle altered the behavior of the sensing element.

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Characterization and anti-bacterial potential of iron oxide nanoparticle processed eco-friendly by plant extract

2020-11-02 , Yan, Leong Poh , Subash Chandra Bose Gopinath , Anbu P. , Farizul Hafiz Kasim , Hanna Ilyani Zulhaimi , Ahmad Radi Wan Yaakub

This research comprehends iron-oxide nanoparticle (IONP) production, the apparent metallic nanostructure with unique superparamagnetic properties. Durian-rind-extract was utilized to synthesize IONP and the color of reaction mixture becomes dark brown, indicated the formation of IONPs and the peak was observed at ∼330 nm under UV-visible spectroscopy. The morphological observation under high-resolution microscopies has revealed the spherical shape and the average size (∼10 nm) of IONP. The further support was rendered by EDX-analysis showing apparent iron and oxygen peaks. XRD results displayed the crystalline planes with (110) and (300) planes at 2θ of 35.73° and 63.53°, respectively. XPS-data has clearly demonstrated the presence of Fe2P and O1s peaks. The IONPs were successfully capped by the polyphenol compounds from durian-rind-extract as evidenced by the representative peaks between 1633 and 595 cm−1 from FTIR analysis. The antimicrobial potentials of IONPs were evidenced by the disk-diffusion assay. The obtained results have abundant attention and being actively explored owing to their beneficial applications.

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In silico structural analysis of truncated 2’ fluoro-RNA aptamer: Elucidating EGF-1 and EGF-2 binding domains on factor IX protein

2021-12-01 , Krishnan H. , Subash Chandra Bose Gopinath , Hanna Ilyani Zulhaimi , Mohd Khairuddin Md Arshad , Subramaniam S.

A stable truncated 2’ fluoro-RNA aptamer contributes to the upstream interruption of the blood coagulation pathway by selectively binding with factor IX protein (FIX). This work followed a rational method for virtually analyzing structural orientation and binding interactions between aptamer and FIX. Three possible aptamer models from the same sequence were designed and evaluated for optimum binding with FIX. Molecular docking was performed to find a prime docking domain and the best docking conformation for a stable aptamer-FIX complex. Possible interactions are observed at PRO126-U9, LYS125-U9, LYS122-A7, ARG116-U9, GLY102-G22, THR101-G22, GLN74-G6, GLY60-G5, CGU36-U11, CGU40-A12, and ASP49-A10. A molecular dynamic simulation assessed the strength of the interaction between aptamer and FIX. It was revealed that the aptamer was effectively bound with the average amino acid fluctuation of 1 Å. The complex reached equilibrium within ten ns during the initial phase of the simulation and then remained stable over 100 ns. B factor analysis showed a moderate atomic displacement from the crystal structure, except at N-terminal from atom 2247−5938. Principal component analysis of post-dynamic trajectories further revealed the stability by the arrayed orientation of amino acids dihedral angles. Overall, 2’ fluoro-RNA aptamer exhibits stronger stability in their interaction with FIX. Noteworthy, the aptamer's stability as an inhibitor to deactivate the clotting cascade by specifically binding with epidermal growth factor-like (EGF) 1 and 2 domains was evidenced.

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