Activation of viruses by host proteases , Activation of viruses by host proteases , کتابخانه‌های دانشگاه کردستان

Activation of viruses by host proteases

Synthesis and evaluation of thiophene-based guanylhydrazones (iminoguanidines) efficient against panel of voriconazole-resistant fungal isolates.

Azines belong to an important class of compounds that are found to have numerous applications in medicinal chemistry. Hydrazones are related to azines and are more widely known compounds that carry many biochemical applications. Hydrazones with appropriate substituents can show azine–hydrazone tautomerism. There are many cases in which azines are wrongly considered to be hydrazones. In this article, we report the tautomeric energy differences of azine and hydrazone and provide the structural details of amidinohydrazones, which prefer azine structure rather than that of hydrazone structure, an important example being the anti-hypertensive drug, guanabenz. The importance of appropriate tautomeric representation of guanabenz has been established in terms of its molecular interactions with a known enzyme.

Azine or hydrazone? The dilemma in amidinohydrazones

p‐Dodecylbenzenesulfonic Acid: An Efficient Brønsted Acid‐Surfactant‐Combined Catalyst to Carry out Diverse Organic Transformations in Aqueous Medium

The replication of numerous pathogenic viruses depends on host proteases, which therefore emerged as potential antiviral drug targets. In some cases, e.g., for influenza viruses, their function during the viral propagation cycle is relatively well understood, where they cleave and activate viral surface glycoproteins. For other viruses, e.g., Ebola virus, the function of host proteases during replication is still not clear. Host proteases may also contribute to the pathogenicity of virus infection by activating proinflammatory cytokines. For some coronaviruses, human proteases can also serve in a nonproteolytical fashion simply as receptors for virus entry. However, blocking of such protein-protein contacts is challenging, because receptor surfaces are often flat and difficult to address with small molecules. In contrast, many proteases possess well-defined binding pockets. Therefore, they can be considered as well-druggable targets, especially, if they are extracellularly active. The number of their experimental crystal structures is steadily increasing, which is an important prerequisite for a rational structure-based inhibitor design using computational chemistry tools in combination with classical medicinal chemistry approaches. Moreover, host proteases can be considered as stable targets, and their inhibition should prevent rapid resistance developments, which is often observed when addressing viral proteins. Otherwise, the inhibition of host proteases can also affect normal physiological processes leading to a higher probability of side effects and a narrow therapeutic window. Therefore, they should be preferably used in combination therapies with additional antiviral drugs. This strategy should provide a stronger antiviral efficacy, allow to use lower drug doses, and minimize side effects. Despite numerous experimental findings on their antiviral activity, no small-molecule inhibitors of host proteases have been approved for the treatment of virus infections, so far.

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The Antiviral Potential of Host Protease Inhibitors

New furin inhibitors based on weakly basic amidinohydrazones

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New furin inhibitors based on weakly basic amidinohydrazones