Researchers have come up with the first high-resolution structure of a molecule that when attached to the genetic material of the hepatitis C virus stops it from reproducing. The structure of the molecule provides a detailed blueprint for the design of drugs that can inhibit the replication of the hepatitis C virus, which proliferates by hijacking the cellular machinery in humans to manufacture duplicate viral particles. Finding a way to stop that process could effectively treat viral infections of hepatitis C, for which no vaccine is currently available. But until now scientists have identified few inhibiting compounds that directly act on the virus's ribonucleic acid (RNA) genome-the organism's full complement of genetic material. "This lack of detailed information on how inhibitors lock onto the viral genome target has hampered the development of better drugs," said Thomas Hermann, an associate professor of chemistry and biochemistry at UC San Diego who headed the research team, which also included scientists from San Diego State University. The team detailed the structure of a molecule that induces the viral RNA to open up a portion of its hinge-like structure and encapsulate the inhibitor like a perfectly fit glove, blocking the ability of the hepatitis C virus to replicate. The molecule is from a class of compounds called benzimidazoles, known to stop the production of viral proteins in infected human cells. Its three-dimensional atomic structure was determined by X-ray crystallography, a method of mapping the arrangement of atoms within a crystal, in which a beam of X-rays strikes a crystal and causes the beam of light to spread. The angles and intensities of the light beams allowed the scientists to calculate the structure of the viral RNA-inhibitor complex. "This structure will guide approaches to rationally design better drug candidates and improve the known benzimidazole inhibitors," said Hermann. "Also, the crystal structure demonstrates that the binding pocket for the inhibitors in the hepatitis C virus RNA resembles drug-binding pockets in proteins. This is important to help overcome the notion that RNA targets are so unlike traditional protein targets that drug discovery approaches with small molecule inhibitors are difficult to achieve for RNA," Hermann added. The study has been published in online edition of the journal Proceedings of the National Academy of Sciences.
GMT 18:35 2018 Thursday ,11 January
Syrian refugee sets himself ablaze at UN office in LebanonGMT 18:48 2018 Tuesday ,09 January
Novo Nordisk woos Belgian nano-drug makerGMT 17:54 2017 Wednesday ,27 December
Medical evacuations begin from besieged Syria rebel bastionGMT 12:14 2017 Monday ,25 December
MoHAP successfully conducts cochlear implant operationGMT 18:24 2017 Sunday ,24 December
Palestinian conjoined twins arrive in RiyadhGMT 19:05 2017 Monday ,18 December
new! magazine names fitness & food editorGMT 17:03 2017 Wednesday ,29 November
Spain reports case of 'mad cow disease'GMT 14:05 2017 Saturday ,11 November
EU can't agree on new licence for controversial glyphosate weedkiller
Maintained and developed by Arabs Today Group SAL.
All rights reserved to Arab Today Media Group 2025 ©
Maintained and developed by Arabs Today Group SAL.
All rights reserved to Arab Today Media Group 2025 ©
Send your comments
Your comment as a visitor