scholarly journals Molecular-docking study of capsular regulatory protein in Streptococcus pneumoniae portends the novel approach to its treatment

2011 ◽  
pp. 131
Author(s):  
Simrika Thapa ◽  
Zubaer
Keyword(s):  
Molecular Docking ◽  
Streptococcus Pneumoniae ◽  
Regulatory Protein ◽  
Docking Study ◽  
The Novel ◽  
Molecular Docking Study ◽  
Novel Approach

scholarly journals Novel Group of AChE Reactivators—Synthesis, In Vitro Reactivation and Molecular Docking Study

Molecules ◽  
2018 ◽  
Vol 23 (9) ◽  
pp. 2291 ◽  
Author(s):  
David Malinak ◽  
Eugenie Nepovimova ◽  
Daniel Jun ◽  
Kamil Musilek ◽  
Kamil Kuca
Keyword(s):  
Molecular Docking ◽  
Molecular Modelling ◽  
Active Site ◽  
Molecular Design ◽  
Docking Study ◽  
The Novel ◽  
Molecular Docking Study ◽  
Causal Treatment ◽  
Modelling Study

The acetylcholinesterase (AChE) reactivators (e.g., obidoxime, asoxime) became an essential part of organophosphorus (OP) poisoning treatment, together with atropine and diazepam. They are referred to as a causal treatment of OP poisoning, because they are able to split the OP moiety from AChE active site and thus renew its function. In this approach, fifteen novel AChE reactivators were determined. Their molecular design originated from former K-oxime compounds K048 and K074 with remaining oxime part of the molecule and modified part with heteroarenium moiety. The novel compounds were prepared, evaluated in vitro on human AChE (HssAChE) inhibited by tabun, paraoxon, methylparaoxon or DFP and compared to commercial HssAChE reactivators (pralidoxime, methoxime, trimedoxime, obidoxime, asoxime) or previously prepared compounds (K048, K074, K075, K203). Some of presented oxime reactivators showed promising ability to reactivate HssAChE comparable or higher than the used standards. The molecular modelling study was performed with one compound that presented the ability to reactivate GA-inhibited HssAChE. The SAR features concerning the heteroarenium part of the reactivator’s molecule are described.

scholarly journals IDENTIFICATION OF NOVEL 5-STYRYL-1,2,4-OXADIAZOLE/TRIAZOLE DERIVATIVES AS THE POTENTIAL ANTI-ANDROGENS THROUGH MOLECULAR DOCKING STUDY

2016 ◽  
Vol 8 (10) ◽  
pp. 72 ◽  
Author(s):  
Paranjeet Kaur ◽  
Gopal L. Khatik
Keyword(s):  
Molecular Docking ◽  
Androgen Receptor ◽  
Binding Affinity ◽  
Docking Study ◽  
Molecular Structures ◽  
The Novel ◽  
Autodock Vina ◽  
Molecular Docking Study ◽  
Triazole Derivatives ◽  
Better Than

<p class="Default"><strong>Objective: </strong>To identify the novel and simple bioactive antiandrogens, that can overcome to side effects as well as drug resistance.</p><p class="Default"><strong>Methods: </strong>The AutoDock Vina (ADT) 1.5.6 software is used for molecular docking purposes. The molecular structures were drawn in ChemBiodraw ultra and by the help of ChemBiodraw 3D, all structures were energy minimized by MM2 method and converted to pdb extension file which is readable at the ADT interface.</p><p class="Default"><strong>Results: </strong>Total ten compounds from both series were shown better binding affinity than <em>R</em>-bicalutamide including oxadiazole and triazole series. Among these pk42 and pk46 were studied in-depth which showed best binding affinity to the androgen receptor. The <em>cis</em>-isomers were found better than their <em>trans</em>-isomer.</p><p><strong>Conclusion: </strong>Novel 5-styryl-1,2,4-oxadiazole/triazole derivatives were studied through molecular modeling using Autodock Vina. The potent compounds which showed better binding affinity than <em>R</em>-bicalutamide like pk24 and 46 were further analyzed for their interactions. The conformational effect also found significant in binding to the androgen receptor.</p>

scholarly journals Molecular-Docking Study of quinazolin-4(3H)-one derivatives against GABAa Receptor Signifies the Novel Approach to Epilepsy Treatment

2020 ◽  
pp. 572-575
Author(s):  
SURAJMAL MALPANI ◽  
Pradeepkumar Mohanty ◽  
Ashish Jain
Keyword(s):  
Molecular Docking ◽  
Docking Study ◽  
Molecular Docking Study ◽  
Antiepileptic Agent ◽  
Protein Targets ◽  
Docking Score ◽  
Novel Approach ◽  
Cns Activity ◽  
Quinazolinone Derivatives

Nowadays, a lot of new active substances as antiepileptic agents have been developed. One of the protein targets of antiepileptic is selective GABA. Selective GABA is the regulator of CNS activity. In this research, quinazolinone derivatives were used to design the antiepileptic agent through a selective GABA activation. The potential activity of quinazolinone derivatives could be increased by substitution in position 3 of quinazolinone. Molecular docking of selective GABA activation was required to predict their antiepileptic activity. The molecular docking of quinazolinone derivatives was carried out using Autodock viva Ver.1.1.2. Twenty quinazolinone derivatives were docked into GABAa with PDB code 4cof. The interaction was evaluated based on the docking score. Diazepam was used as the reference standard for this research. Twenty quinazolinone derivatives showed the approximate docking score -7.1 to -9.3 kcal/mol. All twenty quinazolinone derivatives which value that have greater docking score compared to diazepam used as a standard compound. Derivative Q-18 had higher binding energy than other quinazolinone derivatives because it has the smallest docking score. All new quinazolinone derivatives are feasible to be synthesize and performed their in vitro evaluation.

EVALUATION OF IN-SILICO ANTICANCER POTENTIAL OF PYRETHROIDS: A COMPARATIVE MOLECULAR DOCKING STUDY

2015 ◽  
Author(s):  
Manik Ghosh ◽  
Kamal Kant ◽  
Anoop Kumar ◽  
Padma Behera ◽  
Naresh Rangra ◽  
...  
Keyword(s):  
Molecular Docking ◽  
In Silico ◽  
Docking Study ◽  
Molecular Docking Study

Myricetin Preferentially Binds to Interfacial Regions in Domains 1 – 3 to Inhibit Cholesterol-Dependent Cytolysins: A Molecular Docking Study

2020 ◽  
Author(s):  
Rafael Espiritu
Keyword(s):  
Molecular Docking ◽  
Structural Changes ◽  
Docking Study ◽  
Listeriolysin O ◽  
Molecular Docking Study ◽  
Docking Analysis ◽  
Streptolysin O ◽  
Molecule Inhibitor ◽  
Human Cd59 ◽  
Anthrolysin O

<p>Cholesterol-dependent cytolysins (CDCs) are proteinaceous toxins secreted as monomers by some Gram-positive and Gram-negative bacteria that contribute to their pathogenicity. These toxins bind to either cholesterol or human CD59, leading to massive structural changes, toxin oligomerization, formation of very large pores, and ultimately cell death, making these proteins promising targets for inhibition. Myricetin, and its related flavonoids, have been previously identified as a candidate small molecule inhibitor of specific CDCs such as listeriolysin O (LLO) and suilysin (SLY), interfering with their oligomerization. In this work, molecular docking was performed to assess the interaction of myricetin with other CDCs whose crystal structures are already known. Results indicated that although myricetin bound to the hitherto identified cavity in domain 4 (D4), much more efficient and stable binding was obtained in sites along the interfacial regions of domains 1 – 3 (D1 – D3). This was common among the tested CDCs, which was primarily due to much more extensive stabilizing intermolecular interactions, as indicated by post-docking analysis. Specifically, myricetin bound to (1) the interface of the three domains in anthrolysin O (ALO), perfringolysin O (PFO), pneumolysin (PLY), SLY, and vaginolysin (VLY), (2) at/near the D1/D3 interface in LLO and streptolysin O (SLO), and (3) along the D2/D3 interface in intermedilysin (ILY). These findings provide theoretical basis on the possibility of using myricetin and its related compounds as a broad-spectrum inhibitor of CDCs to potentially address the diseases associated with these pathogens.</p>

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