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Your search keyword '"Norzalina Zakaria"' showing total 3 results
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3 results on '"Norzalina Zakaria"'

1. Mapping Molecular Networks within Clitoria ternatea Linn. against LPS-Induced Neuroinflammation in Microglial Cells, with Molecular Docking and In Vivo Toxicity Assessment in Zebrafish

Author

Nurul Farah Adni Mat Zian, Puspanjali Swain, Siti Munirah Mohd Faudzi, Norzalina Zakaria, Wan Norhamidah Wan Ibrahim, Noraini Abu Bakar, Khozirah Shaari, Johnson Stanslas, Tae-Ik Choi, and Cheol-Hee Kim

Subjects
butterfly pea, Clitoria ternatea, anti-neuroinflammation, Alzheimer’s disease, molecular networking, zebrafish toxicity, Medicine, Pharmacy and materia medica, RS1-441
Abstract

Clitoria ternatea Linn. (CT), or butterfly pea, is an Ayurvedic plant traditionally used as a brain tonic. Recently, it was reported to be of use in treating central nervous system (CNS) disorders, i.e., as an antistress treatment and antidepressant. In the present study, we report a detailed phytochemical profile of the ethyl acetate fraction of the flower of CT (CTF_EA) with significant neuroprotective and anti-neuroinflammatory properties in both LPS-activated BV-2 and SK-N-SH cells. Concurrently, the molecular network (MN) derived from the CTF_EA metabolome allows putative identification of flavonol 3-O-glycosides, hydrocinnamic acids, and primary metabolites. Molecular docking studies suggest that CTF_EA preferentially targets iNOS, resulting in a decrease in nitric oxide (NO). Furthermore, no toxic effects on normal embryonic development, blood vessel formation, and apoptosis are observed when CTF_EA is tested for in vivo toxicity in zebrafish models. The overall preliminary results suggest the anti-neuroinflammatory and neuroprotective effects of CT and provide scientific support for the efficacy of this medicinal plant at local and traditional levels. However, studies on the targeted isolation of bioactive metabolites, in-depth pharmacological efficacy, and safety in mammalian models are urgently needed to expand our understanding of this plant before it is developed into a promising therapeutic agent for brain-related diseases.

Published
2022
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3. In vitro cytotoxicity assay, mushroom tyrosinase inhibitory activity and release analysis of kojic monooleate nanodelivery system and in silico molecular docking study against 2Y9X target enzyme

Author

Muhammad Alif Mohammad Latif, Nur Hana Faujan, Siti Efliza Ashari, Siti Munirah Mohd Faudzi, Hazrina Ab. Hadi, Muhammad Azimuddin Roselan, and Norzalina Zakaria

Subjects
chemistry.chemical_classification, Alanine, Oleic acid, chemistry.chemical_compound, Enzyme, Biochemistry, chemistry, In vivo, Tyrosinase, Protein Data Bank (RCSB PDB), Pharmaceutical Science, Substrate (chemistry), Kojic acid
Abstract

Tyrosinase is the main enzyme that catalyzes the browning of fruits, fungi and vegetables, and melanogenesis process in mammals. Kojic monooleate (KMO) is an ester produced via esterification of kojic acid (KA) with oleic acid and has the potential as a tyrosinase inhibitor. Previously, we have reported the optimization study of the KMO nanoemulsion using Mixture Experimental Design and Response Surface Methodology. This study aims to investigate the in vitro cytotoxicity, tyrosinase inhibitory and release activities of KMO and KMO nanoemulsion. Our study found that both the KMO and KMO nanoemulsion was not cytotoxic against 3T3 mouse embryonic fibroblast cell line with the IC50 > 500 μg/mL. The tyrosinase inhibition assay conducted by using 3,4-dihydroxy phenyl l -alanine ( l -DOPA) substrate revealed a significant potency of KMO (IC50 = 85.98 μM) and its nano-emulsified system (IC50 = 68.20 μg/mL), when compared to KA with the IC50 = 124.28 μM. From Franz cell release study, up to 45.94 ± 0.03% of KMO was released from the nanoemulsion system and diffuses across the cellulose acetate membrane after 8 h of study time, and the kinetic mechanism analysis revealed that the data was most fitted with the zeroth-order model. Moreover, in silico molecular docking was applied to determine binding energy and predict the interaction of mushroom tyrosinase (PDB ID: 2Y9X ) with KMO. The binding energy of the KMO against 2Y9X was −5.70 kcal/mol. The best docked complex was mostly interacted via hydrophobic interaction involving His61, His85, Glu256, His259, Asn260, His263, Phe264, Met280, Gly281, Ser282, Val283, Ala286 residues. Based on the results obtained, the KMO nanoemulsion was suggested to be suitable for use in cosmeceuticals field, and further study through in vivo approach should be carried out to clarify the efficacy and safety of the KMO nanoemulsion.

Published
2021
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