BSc in Biochemistry from Universiti Malaya, Malaysia.
MSc in Biomedicine from Universiti Sains Malaysia, Malaysia
RESEARCH INTERESTS
ANALYTICAL CHEMISTRY AND BIOCHEMISTRY
10
Scopus Publications
Scopus Publications
Structure–Activity-Related Analysis of ACE Inhibitory Peptides Against Furin: A Dual-Action Therapeutic Approach Against SARS-CoV-2 Ainolsyakira Mohd Rodhi, Pei‐Gee Yap, Chee‐Yuen Gan Peptide Science, 2025 The severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2), which is responsible for the COVID‐19 pandemic, enters host cells by binding its spike protein to the angiotensin‐converting enzyme 2 (ACE) receptor on the surface of lung endothelial cells. ACE inhibitors, which were used to manage hypertension, have shown potential to interfere with this viral entry mechanism. This study investigates the dual inhibitory potential of ACE inhibitory peptides against furin, an essential enzyme for the activation of the SARS‐CoV‐2 spike protein. A molecular docking study was performed to identify key interacting amino acid residues at the N‐ and C‐termini that stabilize peptide–furin interactions. Key residues, including ARG, LYS, ALA, and VAL, along with the hydrophobic amino acids PRO, GLY, and LEU, play significant roles in stabilizing these interactions via hydrophobic forces. These residues enhance peptide–enzyme affinity by contributing structural rigidity and flexibility, optimizing binding orientation. The analysis revealed that most ACE inhibitory peptides engage in noncompetitive inhibition by binding to an allosteric site on furin, composed of key residues, such as GLU271, GLY307, SER311, TYR313, LYS449, GLN488, ARG490, ASP530, and ALA532. In vitro and in vivo studies are necessary to further evaluate the therapeutic safety and efficacy of these peptides, paving the way for innovative treatment strategies against COVID‐19.
Exploring α-Glucosidase Inhibitory Peptides: Structure-Activity Relationship Analysis and Perspectives for Designing Potential Anti-Diabetic Agents Ainolsyakira Mohd Rodhi, Pei Gee Yap, Olusegun Abayomi Olalere, Chee Yuen Gan Jundishapur Journal of Natural Pharmaceutical Products, 2023 Context: α-Glucosidase (AG) inhibitory peptides represent a promising new class of therapeutic agents for the treatment of diabetes. However, there is a need to further understand the mechanisms and properties of these peptides. Evidence Acquisition: In this comprehensive review, AG inhibitory peptides were categorized into three groups based on their length: short, medium, and long peptides. Data from the BioPEP-UWM database and recent publications were gathered to conduct a structure-activity relationship analysis for these peptides, focusing on identifying their reactive residues and AG binding sites. Results: Through extensive examination, five substrate analogs (Trp376, Asp404, Ile441, Met519, and Phe649) and two catalytic residues (Asp518 and Asp616) were identified as the preferred inhibitory sites on AG. Furthermore, amino acid preferences and their positionings at different terminals on peptides, including the ultimate (N1 and C1), penultimate (N2 and C2), and antepenultimate (N3 and C3), were explored. Our findings revealed that these peptides were predominantly hydrophobic and tended to contain hydrophobic amino acids with hydrophobic alkyl/aryl side chains (such as lysine, glutamine, proline, and/or arginine). To gain further insights into peptide-AG interactions, docking analysis was performed, which highlighted the significance of hydrophobic bonds as the primary mode of interaction. Conclusions: By pooling all the findings, this review provided essential and practical information for the design and discovery of peptide-based anti-diabetic agents.
A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis Ainolsyakira Mohd Rodhi, Pei-Gee Yap, Olalere Olusegun Abayomi, Chee-Yuen Gan Food Chemistry Advances, 2023 This review focused on assessing the type of amino acids at terminal positions of previously reported DPPIV inhibitory peptides to predict the key feature of sequences that specifically target DPPIV. Thorough understanding on side chain property of reactive amino acids and its contribution on DPPIV recognition and binding was acquired through structure-activity relationship and molecular docking analysis. Overall, N-terminals dominant by Leu, Pro, Ile, Phe, Ala, Tyr and/or Gly, whereas C-terminals dominant by Arg, Phe, Met, Ala, Val, Pro, Gln, Ile, Glu, Leu and/or Lys depending on the peptide length and terminal positions where these reactive residues hydrophobically interacted with the catalytic (Ser630) or substrate-binding (Tyr629, Tyr547, Tyr666 and Phe357) hotspots of DPPIV. Molecular docking prediction also suggested the presence of secondary hotspots (Arg125, His126, Gly355, Pro359, Ile405, Asp545, Val546, Cys551, Cys552, Gln553, Trp627, Tyr662, Ala707, Asp709, Glu738, Asp739, Gly741, Ile742 and Tyr752) to support peptide binding. In conclusion, outcome of the current review could inspire the design of potent DPPIV inhibitory peptides where the preference for hydrophobic and aliphatic reactive amino acids could be translated into candidate DPPIV-targeting sequences given their ability to engage with DPPIV hotspots.
A comprehensive review on the pancreatic lipase inhibitory peptides: A future anti-obesity strategy Tan Yong Chia, Chee-Yuen Gan, Muhammad Hakimin Shafie, Pei Gee Yap, Ainolsyakira Mohd Rodhi, Ashfaq Ahmad, Vikneswaran Murugaiyah, Mohammed H Abdulla, Edward James Johns Electronic Journal of General Medicine, 2023 Dysregulation of lipid homeostasis contributes to obesity and can directly lead to several critical public health concerns globally. This paper aimed to present a brief review of related properties and the use of pancreatic lipase inhibitors as the future weight loss drug discovery and development procured from a wide range of natural sources. A total of 176 pancreatic lipase inhibitory peptides were identified from recent publications and peptide databases. These peptides were classified into three categories according to their peptide length and further analyzed using bioinformatic approaches to identify their structural activity relationship. Molecular docking analyses were conducted for each amino acid at the terminal position of the peptides to predict the binding affinity between peptide-enzyme protein complexes based on intermolecular contact interactions. Overall, the observations revealed the features of the inhibitory peptides and their inhibitory mechanisms and interactions. These findings strived to benefit scientists whose research may be relevant to anti-obesity drug development and/or discovery thereby support effective translation of preclinical research for humans’ health being.
Adulteration Detection of Edible Bird’s Nests Using Rapid Spectroscopic Techniques Coupled with Multi-Class Discriminant Analysis Jing Sheng Ng, Syahidah Akmal Muhammad, Chin Hong Yong, Ainolsyakira Mohd Rodhi, Baharudin Ibrahim, Mohd Noor Hidayat Adenan, Salmah Moosa, Zainon Othman, Nazaratul Ashifa Abdullah Salim, Zawiyah Sharif, Faridah Ismail, Simon D. Kelly, Andrew Cannavan Foods, 2022 Edible bird’s nests (EBNs) are vulnerable to adulteration due to their huge demand for traditional medicine and high market price. Presently, there are pressing needs to explore field-deployable rapid screening techniques to detect adulteration of EBNs. The objective of this study is to explore the feasibility of using a handheld near-infrared (VIS/SW-NIR) spectroscopic device for the determination of EBN authenticity against the benchmark performance of a benchtop mid-infrared (MIR) spectrometer. Forty-nine authentic EBNs from the different states in Malaysia and 13 different adulterants (five types) were obtained and used to simulate the adulteration of EBNs at 1, 5 and 10% adulteration by mass (a total of 15 adulterated samples). The VIS/SW-NIR and MIR spectra collated were subsequently processed, modelled and classified using multi-class discriminant analysis. The VIS/SW-NIR results showed 100% correct classification for the collagen and nutrient agar classes in authenticity classification, while for the other classes, the lowest correct classification rate was 96.3%. For MIR analysis, only the karaya gum class had 100% correct classification whilst for the other four classes, the lowest rate of correct classification was at 94.4%. In conclusion, the combination of spectroscopic analysis with chemometrics can be a powerful screening tool to detect EBN adulteration.
Addressing the unfulfilled codex standard for honey for stingless bee honey through lyophilization Chin-Hong Yong, Syahidah Akmal Muhammad, Widad Fadhullah, Hasnuri Mat Hassan, Ainolsyakira Mohd Rodhi, Mohd Zulkifli Mustafa, Simon D. Kelly Isotopes in Environmental and Health Studies, 2022 Some studies have found that the nutritional values of stingless bee honey (SBH) may be similar if not more than normal honey, prompting the Malaysian government to promote it as a superfood. However, SBH does not fulfil the Codex Standard for Honey (CODEX STAN 12-19811) in terms of moisture content and the lack of protein to be analysed with Internal Standard Carbon Isotope Ratio Analysis (ISCIRA). Hence, a lyophilization process was introduced prior to stable carbon isotope analysis of SBH to address both of these issues. It was found that once moisture content was decreased to a level below 20 % for 19 SBH samples, the percentage increment of protein extracted from the samples varied between 6 and 385 % relative to protein extracted from SBH before lyophilization with nine samples found to be adulterated. Caution is necessary when lyophilizing the SBH as significant isotope shifts were seen for SCIRA and ISCIRA values. Nevertheless, the carbon isotope shifts did not change the final outcome of the ‘pass’ or ‘fail’ of the adulteration result. Overall, the removal of water from SBH is required but caution is necessary as carbon isotope shifts were observed as SBHs underwent the lyophilization process.
