Biological Investigation of 2-Thioxo-benzo[g]quinazolines against Adenovirus Type 7 and Bacteriophage Phi X174: An In Vitro Study

Mortality and morbidity caused by viruses are a global health problems. Therefore, there is always a need to create novel therapeutic agents and refine existing ones to maximize their efficacy. Our lab has produced benzoquinazolines derivatives that have proven effective activity as antiviral compou...

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Published inCurrent Issues in Molecular Biology Vol. 45; no. 5; pp. 3787 - 3800
Main Authors Abuelizz, Hatem A, Bakheit, Ahmed H, Marzouk, Mohamed, El-Senousy, Waled M, Abdellatif, Mohamed M, Ali, Essam E, Mostafa, Gamal A E, Al-Salahi, Rashad
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 28.04.2023
MDPI
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Summary:Mortality and morbidity caused by viruses are a global health problems. Therefore, there is always a need to create novel therapeutic agents and refine existing ones to maximize their efficacy. Our lab has produced benzoquinazolines derivatives that have proven effective activity as antiviral compounds against herpes simplex (HSV 1 and 2), coxsackievirus B4 (CVB4), and hepatitis viruses (HAV and HCV). This in vitro study was aimed at investigating the effectiveness of benzoquinazoline derivatives - against adenovirus type 7 and bacteriophage phiX174 using a plaque assay. The cytotoxicity against adenovirus type 7 was also performed in vitro, using a MTT assay. Most of the compounds exhibited antiviral activity against bacteriophage phiX174. However, compounds , , , and showed statistically significant reductions of 60-70% against bacteriophage phiX174. By contrast, compounds , , , , , and were ineffective against adenovirus type 7, and compounds and had remarkable efficacy (50%). Using the MOE-Site Finder Module, a docking study was carried out in order to create a prediction regarding the orientation of the lead compounds ( , , and ). This was performed in order to investigate the activity of the lead compounds , , and against the bacteriophage phiX174 by locating the ligand-target protein binding interaction active sites.
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ISSN:1467-3045
1467-3037
1467-3045
DOI:10.3390/cimb45050244