Asmaa Zainal Abidin
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Asmaa Zainal Abidin has a total of 16 co-authors. Here are the top co-authors by number of shared publications:
- Osamah Aldaghri
Department of Physics, College of Sciences, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh 13318, Saudi Arabia
2 shared publications - Zakariyya Uba Zango
Department of Chemistry, College of Natural and Applied Science, Al-Qalam University Katsina, Katsina, Nigeria
2 shared publications Abdelmoneim Sulieman
1 shared publication- Hanan Akhdar
Physics Department, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh, Saudi Arabia
1 shared publication - Hui Suan Ng
Centre for Research and Graduate Studies, University of Cyberjaya, Cyberjaya, Malaysia
1 shared publication Jun Wei Lim
1 shared publication
Latest Publications
- 6 June 2024
- Published by World Scientific Pub Co Pte Ltd in Journal of Molecular and Engineering Materials
- Vol. 13 (01)
Molecular Docking and Ligand-Binding Analysis of Amidine Derivatives Targeting Pseudomonas aeruginosa and Escherichia coli Bacterial Strains: An In Silico Approach
Gram-negative bacteria represent a formidable challenge due to their exhibition of elevated resistance to various antibiotics. This study delves into the crisis posed by antimicrobial resistance (AMR), focusing on the alarming rise of bacteria (Gram-negative), such as Escherichia coli (E. coli) and Pseudomonas aeruginosa (P. aeruginosa), notorious for their severe infections. By examining the binding interaction with antibiotics (ampicillin, ciprofloxacin, trimethoprim, pentamidine, furamidine, and oligoamidine) and bacterial protein targets, the study utilized molecular docking and ligand-binding analysis. The result reveals different LibDock scores with the bacterial strain. Higher scores indicate stronger binding. Pentamidine exhibited the highest scores with all bacterial strains. CDOCKER energy due to interaction was computed to analyze the molecules binding with the bacteria, and pentamidine stood with higher CDOCKER value, indicating strong binding affinity. The work also assessed the antibiotics likeness using the rule of Lipinski’s five (RO5), and several antibiotics conform to the criteria. Molecular dynamics simulations were conducted to estimate compound stabilities, revealing stable conformations. The results revealed a stable potential energy (PE) profile for 5V7A Chain B. The RMSD profiles exhibited deviations within certain time intervals, indicating potential conformational changes in the antibiotics.
- 6 June 2024
- Published by World Scientific Pub Co Pte Ltd in Journal of Molecular and Engineering Materials
- Vol. 13 (01)
Molecular Docking and Ligand-Binding Analysis of Amidine Derivatives Targeting Pseudomonas aeruginosa and Escherichia coli Bacterial Strains: An In Silico Approach
Gram-negative bacteria represent a formidable challenge due to their exhibition of elevated resistance to various antibiotics. This study delves into the crisis posed by antimicrobial resistance (AMR), focusing on the alarming rise of bacteria (Gram-negative), such as Escherichia coli (E. coli) and Pseudomonas aeruginosa (P. aeruginosa), notorious for their severe infections. By examining the binding interaction with antibiotics (ampicillin, ciprofloxacin, trimethoprim, pentamidine, furamidine, and oligoamidine) and bacterial protein targets, the study utilized molecular docking and ligand-binding analysis. The result reveals different LibDock scores with the bacterial strain. Higher scores indicate stronger binding. Pentamidine exhibited the highest scores with all bacterial strains. CDOCKER energy due to interaction was computed to analyze the molecules binding with the bacteria, and pentamidine stood with higher CDOCKER value, indicating strong binding affinity. The work also assessed the antibiotics likeness using the rule of Lipinski’s five (RO5), and several antibiotics conform to the criteria. Molecular dynamics simulations were conducted to estimate compound stabilities, revealing stable conformations. The results revealed a stable potential energy (PE) profile for 5V7A Chain B. The RMSD profiles exhibited deviations within certain time intervals, indicating potential conformational changes in the antibiotics.