Mohammad Reza Bozorgmehr Articles List

List of Articles Mohammad Reza Bozorgmehr

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1 - Effect of Linear and Cyclic Lysine-Lysine-Tryptophan- Tryptophan -Lysine-Phenylalanine Antimicrobial Peptide on Sodium Dodecyl Sulfate Micelle as Cell Membrane Mimetic: Molecular Dynamics Simulation Study
S. Hassan Mortazavi Mohammad Reza Bozorgmehr Mohammad Momen Heravi
10.22034/jchr.2022.1955430.1533

Drug resistance has limited the synthesis of new antibiotics. Therefore, the use of compounds that do not have drug resistance has been considered. Antimicrobial peptides are among the compounds for which drug resistance has not been reported. On the other hand, it has More

Drug resistance has limited the synthesis of new antibiotics. Therefore, the use of compounds that do not have drug resistance has been considered. Antimicrobial peptides are among the compounds for which drug resistance has not been reported. On the other hand, it has been found that the activity of these compounds is less than that of antibiotics. Therefore, the design of appropriate antimicrobial peptides is challenging. To address this challenge, efforts have been made to understand their mechanism of action. However, their mechanism of action is not well understood. In this work, the interaction of two cyclic and linear antimicrobial peptides with sodium dodecyl sulfate micelles as cell membrane mimetics method has been studied by molecular dynamics simulation. The micellar radius of gyration shows good agreement with the experimental results and the results of other simulations performed. Calculation of the conformational factor shows that cyclic antimicrobial peptide has a greater affinity for interaction with micelles. Charged and aromatic residues are involved in the interaction of cyclic antimicrobial peptides with micelles. Whereas, only charged residues are effective in the interaction of the linear antimicrobial peptides with micelle. Manuscript profile
Open Access Article
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2 - New Imidazo[4,5-a] Acridine: Synthesis and Studying the Molecular Dynamics Simulation of Its Interaction with the Topoisomerase Enzyme
Maryam Toosi Mehdi Pordel Mohammad Reza Bozorgmehr
10.22034/jchr.2023.1984058.1724

Acridine and imidazole were combined and synthesized 3,8-disubstituted-propyl-3H-imidazo[4,5-a]acridine-11-carbonitrile, as a new derivative. The interaction of this new compound with the topoisomerase enzyme was studied by molecular dynamics simulation. The 3,8-disubst More

Acridine and imidazole were combined and synthesized 3,8-disubstituted-propyl-3H-imidazo[4,5-a]acridine-11-carbonitrile, as a new derivative. The interaction of this new compound with the topoisomerase enzyme was studied by molecular dynamics simulation. The 3,8-disubstituted-3H-imidazo[4,5-a]acridine-11-carbonitrile structure has been optimized by the density functional theory method. According to the results obtained from the molecular dynamics simulation, Arg364, Lys532, Asp533, Tyr537, Arg590, Cys630, Asn631, Gln633 and Adenine11 interact with the ligand by hydrophobic interactions and Arg488 and Adenine12 interact with the ligand by hydrogen bond interactions. Due to the fact that some of these residues, Arg488 and Arg590 are located in the enzyme active site, the new ligand appears to be inhibitory effect. Also, the calculation of the Harmonic Oscillator Model for Aromaticity (HOMA) index showed that the 5-membered ring of ligand and the 6-membered ring attached to the 5-membered ring had more reactivity with the enzyme. The contribution of charged residues in the binding free energy of the ligand is greater than the uncharged residues. Manuscript profile

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List of Articles Mohammad Reza Bozorgmehr