Qosay Al-Balas
Jordan University of Science and Technology
59 Papers
61 Citations
Qosay Al-Balas is an academic researcher from Jordan University of Science and Technology. The author has contributed to research in topics: Antimicrobial & Chemistry. The author has an hindex of 13, co-authored 48 publications. Previous affiliations of Qosay Al-Balas include Strathclyde Institute of Pharmacy and Biomedical Sciences & University of Jordan.
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Papers
Molecular docking and dynamic studies of a potential therapeutic target inhibiting glyoxalase system: Metabolic action of the 3, 3 '- [3- (5-chloro-2-hydroxyphenyl) -3-oxopropane-1, 1-diyl] - Bis-4-hydroxycoumarin leads overexpression of the intracellular level of methylglyoxal and induction of a pro-apoptotic phenomenon in a hepatocellular carcinoma model
Nadia Taibi,Qosay Al-Balas,Nadjia Bekari,Oualid Talhi,Ghazi A. Al Jabal,Yasmine Benali,Rachid Ameraoui,Mohamed Hadjadj,Amina Taïbi,Zahra Mouna Boutaiba,Mohamed Abou-mustapha,Farida Khammar,Fayçal Dergal,Ridha Hassaine,Leila Boukenna,Khaldoun Bachari,Artur M. S. Silva +16 more
TL;DR: In this article, the authors demonstrate the inhibitory effect of 3, 3'-[3-(5-chloro-2-hydroxyphenyl)-3-oxopropane-1, 1-diyl] Bis (4-hydroxycoumarin) on the glyoxalase system, and indirectly its anticancer activity.
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In vivo antimicrobial activity of the hybrid peptide H4: a follow-up study.
TL;DR: A novel hybrid peptide named H4 is designed that exhibits potent antimicrobial activity and low toxicity in vitro and evaluated the in vivo activity and toxicity of H4 against Staphylococcus aureus peritonitis mice model to indicate the potential therapeutic efficacy and safety of the peptide.
Identification of Human Leukotriene A4 Hydrolase Inhibitors Using Structure-Based Pharmacophore Modeling and Molecular Docking.
Suaad A. Audat,Nizar A. Al-Shar’i,Buthina A. Al-Oudat,Amanda C. Bryant-Friedrich,Mel F. Bedi,Aref Zayed,Qosay Al-Balas +6 more
TL;DR: The results were very promising, with the most active compound showing 73.6% inhibition of the basal epoxide hydrolase activity of LTA4H, providing valuable information for the design and development of more potent and selective inhibitors.
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•Journal Article
Identification of Possible Glyoxalase II Inhibitors as Anticancer Agents by a Customized 3D Structure-Based Pharmacophore Model
TL;DR: This work is the first study that aims to find none-glutathione-based inhibitors of the glyoxalase-II enzyme as potential anticancer drugs based on computer aided drug design and is a hybrid of three complementary 3D pharmacophores.
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