Aims and Scope

The Open Biochemistry Journal is an open-access online journal dedicated to the rapid publication of original research articles, reviews/mini-reviews, letters and guest edited single topic issues in all sub-disciplines of biochemistry (including genomics, gene expression, replication, proteomics, structural biology, enzymology, bioenergetics, metabolism, signal transduction, bioinformatics, cell biology, glycoscience, glycobiology, glycochemistry, glycotechnology, pharmacology, enzyme inhibition, inhibitory processes, immunochemistry, macromolecules, biopolymers, and nitric oxide). The journal publishes clearly written articles describing significant advances in the field that are of great interest for the scientific community worldwide. Non-conclusive or confirmatory studies are not accepted.


Recent Articles

COVID-19: Mechanisms of the Antiviral Activities of Selective Antibiotics Targeting the Human 80S Ribosome

Codjo Hountondji, Jacques H. Poupaert, Blanche Aguida, Fulbert K. Agbo Saga, Joël Pothier, Jean-Bernard Créchet, Cédrick Cocks, Lionel Barty, Urbain C. Kassehin, Fernand A. Gbaguidi

Background:

The majority of scientists, physicians, and healthcare professionals were trained with the paradigm: “antibiotics are for bacteria only !”, because they misunderstood the definition of the ribosome targeting antibiotics. In the context of the current worldwide COVID-19 pandemic, it might be useful to recall as precisely as possible the definition of the word antibiotic and provide evidence that some classes of antibiotics could offer excellent means to counteract viral infections via specific mechanisms.

Methods:

Molecular modeling and docking studies were used, as well as the tRNAox labeling reaction of the ribosomal protein eL42 in situ on human 80S ribosomes to demonstrate that cycloheximide and its thiosemicarbazone analogues bind to the catalytic Lys-53 residue of the human large subunit ribosomal protein eL42.

Results:

Comparison of the binding sites for Cycloheximide (CHX) and Sparsomycin (SPS) on the evolutionarily conserved E. coli bL12 and S. cerevisiae eL42 by means of molecular modeling and docking studies showed that: (i) SPS binds in proximity to the catalytic Lys-65 residue of the GANK motif of rp bL12 and to the catalytic Lys-55 residue of the GGQTKP motif of rp eL42; (ii) CHX failed to bind to the GANK motif, while the glutarimide moiety of SPS and CHX was found to make contact with Lys-55 of the GGQTKP motif of rp eL42.

Conclusion:

In this report, we demonstrate that cycloheximide and its thiosemicarbazone analogues are capable of inhibiting the human 80S ribosomes selectively through their binding to the ε-amino group of the side chain of Lys-53. As a consequence, these small-molecule inhibitors of translation are susceptible to exhibit antiviral activities by preventing the human ribosomes of the SARS-CoV-2 infected cells from synthesizing the viral proteins and enzymes.


October 05, 2021
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Editor's Choice

Study of the Interaction of Zinc Cation with Azithromycin and its Significance in the COVID-19 Treatment: A Molecular Approach

Jacques H. Poupaert, Blanche Aguida, Codjo Hountondji

Introduction:

On account of the current COVID-19 pandemic, we have explored the importance of azithromycin and zinc in the treatment of the coronavirus disease by studying the interaction between the cation Zn++ and azithromycin with the tools of the semi-empirical quantum mechanics PM3 method.

Methods:

By this approach, the niche in which Zn++ is located was determined. Zn++ creates a strong clastic binding between an amine and a hydroxyl group located on the amino-hexose side-chain. Such an interaction serves as a shuttle and allows zinc cation to invade endocellular structures.

Results:

In this triple collaborative association, the role of hydroxychloroquine would be more that of a chaotropic agent at plasmic membranes, which facilitates access to the azithromycin-Zn++ equipage into key internal compartments.

Conclusion:

Finally, we show that both azithromycin and Zn++ are susceptible to play a direct role against the replication and the assembly of SARS-CoV-2 particles.


September 22, 2020
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