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Leaky Scanning

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...

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Related Experiment Video

Updated: Mar 7, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Protein-Linker Co-engineering for Broad-Spectrum Antiviral Development against Enveloped Viruses.

Lixia Wei^1,2, Colleen N Loynachan¹, Gregory Mathez³

¹Institute of Materials Science and Engineering, École polytechnique fédérale de Lausanne, Lausanne 1015, Switzerland.

ACS Materials Letters

|March 6, 2026

Summary

This summary is machine-generated.

Scientists developed a new method to create broad-spectrum, nontoxic antivirals by modifying natural proteins. This versatile platform shows promise for rapid development against current and future viral threats.

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Last Updated: Mar 7, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance

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Published on: June 14, 2022

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Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16

Use of Viral Entry Assays and Molecular Docking Analysis for the Identification of Antiviral Candidates against Coxsackievirus A16

Published on: July 15, 2019

Area of Science:

Biochemistry
Virology
Drug Discovery

Background:

Emerging and re-emerging viruses pose significant global health risks.
Broad-spectrum antivirals are crucial for pandemic preparedness.
Existing antiviral strategies face challenges with resistance and specificity.

Purpose of the Study:

To develop a general and simple strategy for creating broad-spectrum, nontoxic antiviral agents.
To functionalize natural proteins into effective antiviral compounds.
To evaluate the efficacy and mechanism of these modified proteins against enveloped viruses.

Main Methods:

Chemical functionalization of natural proteins via one-step conjugation with alkyl ligands terminated by secondary amines.
In vitro testing of functionalized proteins against Herpes Simplex Virus 2 (HSV-2), Influenza A H1N1, and SARS-CoV-2.
Assessment of antiviral activity, ligand density effects, alkyl chain length impact, and performance in serum environments.

Main Results:

Functionalized proteins demonstrated potent inhibition against HSV-2, Influenza A H1N1, and SARS-CoV-2 (EC50 in nanomolar to micromolar range).
Antiviral efficacy correlated positively with ligand density and alkyl chain length.
Longer alkyl chains shifted activity from reversible (virustatic) to irreversible (virucidal).
The antiviral compounds maintained robust performance in complex serum environments and were most effective prophylactically.

Conclusions:

A versatile and simple protein functionalization strategy yields broad-spectrum, nontoxic antivirals.
This platform offers a promising approach for rapid antiviral development against diverse viral threats.
The modified proteins present a viable first line of defense against emerging and re-emerging viruses.