Saharuddin Bin Mohamad

Dr. Saharuddin Bin Mohamad


Research Focus & Metrics

Academic Career Length

19Years (2008-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
Verified
Journal Article
Open access
PDF file
OHOmer Hamdi
Omer Hamdi
SFShevin Rizal Feroz
Shevin Rizal Feroz
JSJamil A. Shilpi
Jamil A. Shilpi
EAEl Hassane Anouar
El Hassane Anouar
AMAbdul Kadir Mukarram
Abdul Kadir Mukarram
KAKhalijah Awang
Khalijah Awang
Curcumenol and curcumenone are two major constituents of the plants of medicinally important genus of Curcuma, and often govern the pharmacological effect of these plant extracts. These two compounds, isolated from C. zedoaria rhizomes were studied for their binding to human serum albumin (HSA) using the fluorescence quench titration method. Molecular docking was also performed to get a more detailed insight into their interaction with HSA at the binding site. Additions of these sesquiterpenes to HSA produced significant fluorescence quenching and blue shifts in the emission spectra of HSA. Analysis of the fluorescence data pointed toward moderate binding affinity between the ligands and HSA, with curcumenone showing a relatively higher binding constant (2.46 × 105 M−1) in comparison to curcumenol (1.97 × 104 M−1). Cluster analyses revealed that site I is the preferred binding site for both molecules with a minimum binding energy of −6.77 kcal·mol−1. However, binding of these two molecules to site II cannot be ruled out as the binding energies were found to be −5.72 and −5.74 kcal·mol−1 for curcumenol and curcumenone, respectively. The interactions of both ligands with HSA involved hydrophobic interactions as well as hydrogen bonding.

1 January 2014 in The Scientific World Journal
Verified
Journal Article
Open access
PDF file
HMHoda Mirsafian
Hoda Mirsafian
ARAdiratna Binti Mat Ripen
Adiratna Binti Mat Ripen
ASAarti Singh
Aarti Singh
PTPhaik Hwan Teo
Phaik Hwan Teo
AMAmir Feisal Merican
Amir Feisal Merican
SMSaharuddin Bin Mohamad
Saharuddin Bin Mohamad
Synonymous codon usage bias is an inevitable phenomenon in organismic taxa across the three domains of life. Though the frequency of codon usage is not equal across species and within genome in the same species, the phenomenon is non random and is tissue-specific. Several factors such as GC content, nucleotide distribution, protein hydropathy, protein secondary structure, and translational selection are reported to contribute to codon usage preference. The synonymous codon usage patterns can be helpful in revealing the expression pattern of genes as well as the evolutionary relationship between the sequences. In this study, synonymous codon usage bias patterns were determined for the evolutionarily close proteins of albumin superfamily, namely, albumin,α-fetoprotein, afamin, and vitamin D-binding protein. Our study demonstrated that the genes of the four albumin superfamily members have low GC content and high values of effective number of codons (ENC) suggesting high expressivity of these genes and less bias in codon usage preferences. This study also provided evidence that the albumin superfamily members are not subjected to mutational selection pressure.

1 February 2020 in Clinical Immunology
Verified
Journal Article
Open access
CCChai Teng Chear
Chai Teng Chear
RNRevathy Nallusamy
Revathy Nallusamy
SCScott W. Canna
Scott W. Canna
KCKwai Cheng Chan
Kwai Cheng Chan
MBMohd Farid Baharin
Mohd Farid Baharin
SMSaharuddin Bin Mohamad
Saharuddin Bin Mohamad
Autoinflammatory disorders are characterized by dysregulated innate immune response, resulting in recurrent uncontrolled systemic inflammation and fever. Gain-of-function mutations in NLRC4 have been described to cause a range of autoinflammatory disorders. We report a twelve-year-old Malay girl with recurrent fever, skin erythema, and inflammatory arthritis. Whole exome sequencing and subsequent bidirectional Sanger sequencing identified a heterozygous missense mutation in NLRC4 (NM_001199138: c.1970A > T). This variant was predicted to be damaging in silico, was absent in public and local databases and occurred in a highly conserved residue in the leucine-rich repeat (LRR) domain. Cytokine analysis showed extremely high serum IL-18 and IL-18/CXCL9 ratio, consistent with other NLRC4-MAS patients. In summary, we identified the first patient with a novel de novo heterozygous NLRC4 gene mutation contributing to autoinflammatory disease in Malaysia. Our findings reinforce the likely pathogenicity of specific LRR domain mutations in NLRC4 and expand the clinical spectrum of NLRC4 mutations.

10 April 2017 in Natural Product Research
Verified
Journal Article
Closed access
ABAmirul Ridzuan Abu Bakar
Amirul Ridzuan Abu Bakar
TMThamilvaani Manaharan
Thamilvaani Manaharan
AMAmir Feisal Merican
Amir Feisal Merican
SMSaharuddin Bin Mohamad
Saharuddin Bin Mohamad
Ficus deltoidea leaves extract are known to have good therapeutic properties such as antioxidant, anti-inflammatory and anti-diabetic. We showed that 50% ethanol-water extract of F. deltoidea leaves and its pungent compounds vitexin and isovitexin exhibited significant (p < 0.05) α-amylase inhibition with IC50 (vitexin: 4.6 μM [0.02 μg/mL]; isovitexin: 0.06 μg/mL [13.8 μM] and DPPH scavenging with IC50 (vitexin: 92.5 μM [0.4 μg/mL]; isovitexin: 0.5 μg/mL [115.4 μM]). Additionally, molecular docking analysis confirmed that vitexin has a higher binding affinity (-7.54 kcal/mol) towards α-amylase compared to isovitexin (−5.61 kcal/mol). On the other hand, the molecular dynamics findings showed that vitexin-α-amylase complex is more stable during the simulation of 20 ns when compared to the isovitexin-α-amylase complex. Our results suggest that vitexin is more potent and stable against α-amylase enzyme, thus it could develop as a therapeutic drug for the treatment of diabetes.

11 April 2022 in Nutrients
Verified
Journal Article
Open access
PDF file
BTBP Teh
BP Teh
NANorzahirah Ahmad
Norzahirah Ahmad
SMSaharuddin Bin Mohamad
Saharuddin Bin Mohamad
TTTerence Yew Chin Tan
Terence Yew Chin Tan
MRMohd Ridzuan Mohd Abd Razak
Mohd Ridzuan Mohd Abd Razak
AMAmi Fazlin FAZLIN BT. SYED Syed Mohamed
Ami Fazlin FAZLIN BT. SYED Syed Mohamed
The potential therapeutic effect of Carica papaya leaf juice has attracted wide interest from the public and scientists in relieving dengue related manifestations. Currently, there is a lack of evaluated evidence on its juice form. Therefore, this scoping review aims to critically appraise the available scientific evidence related to the efficacy of C. papaya leaf juice in dengue. A systematic search was performed using predetermined keywords on two electronic databases (PubMed and Google Scholar). Searched results were identified, screened and appraised to establish the association between C. papaya and alleviating dengue associated conditions. A total of 28 articles (ethnobotanical information: three, in vitro studies: three, ex vivo studies: one, in vivo study: 13, clinical studies: 10) were included for descriptive analysis, which covered study characteristics, juice preparation/formulations, study outcomes, and toxicity findings. Other than larvicidal activity, this review also reveals two medicinal potentials of C. papaya leaf juice on dengue infection, namely anti-thrombocytopenic and immunomodulatory effects. C. papaya leaf juice has the potential to be a new drug candidate against dengue disease safely and effectively.

1 January 2014 in The Scientific World Journal
Verified
Journal Article
Open access
PDF file
HMHoda Mirsafian
Hoda Mirsafian
ARAdiratna Binti Mat Ripen
Adiratna Binti Mat Ripen
AMAmir Feisal Merican
Amir Feisal Merican
SMSaharuddin Bin Mohamad
Saharuddin Bin Mohamad
Beta-amyloid precursor protein cleavage enzyme 1 (BACE1) and beta-amyloid precursor protein cleavage enzyme 2 (BACE2), members of aspartyl protease family, are close homologues and have high similarity in their protein crystal structures. However, their enzymatic properties differ leading to disparate clinical consequences. In order to identify the residues that are responsible for such differences, we used evolutionary trace (ET) method to compare the amino acid conservation patterns of BACE1 and BACE2 in several mammalian species. We found that, in BACE1 and BACE2 structures, most of the ligand binding sites are conserved which indicate their enzymatic property of aspartyl protease family members. The other conserved residues are more or less randomly localized in other parts of the structures. Four group-specific residues were identified at the ligand binding site of BACE1 and BACE2. We postulated that these residues would be essential for selectivity of BACE1 and BACE2 biological functions and could be sites of interest for the design of selective inhibitors targeting either BACE1 or BACE2.