A joint medical study on an anti-Aids drug by the US
and Bangkok City Hall has hinted on the need to address again the
problem with health costs and, more importantly, the political
toxic...
The facts are simple, and they are politically intimidating. There really are only two that matter. First, the study proved beyond doubt that the drug Tenofovir stops HIV infections to more than half of the abusers who inject heroin, methamphetamine and other illicit drugs.
The study represents a new use for Tenofovir, which is already a
well-known anti-AIDS drug often prescribed alone or in cocktails for
those with HIV or AIDS. But the study's conclusion that it is an
effective preventative lends new status to the medication.
In Thailand, where a few cases of compulsory licensing in 2007 caused massive trade and diplomatic problems, Tenofovir is in a kind of legal limbo. While it has not been submitted for CL, neither has it
won a Thai patent, a step needed to legalize that 428,000 baht-per-patient cost.
The Tenofovir used in the field study with drug abusers was produced by the Government Pharmaceutical Organization (GPO). Despite a somewhat murky legal status, it is available at some pharmacies, hospitals etc.
In their discovery of a new way to inhibit formation of HIV’s protease enzyme, scientists may have identified a new drug target, according to new data published in the August 2008 issue of Biopolymers.
Protease is a doughnut-shaped enzyme involved in processing viral proteins and assembling them into new infectious viruses.
It is currently the target of a handful of drugs called protease inhibitors, all of which bind to and block the hole in the doughnut shape.
Heather Carlson, PhD, a professor of chemistry at the University of Michigan, and her colleagues used computer models of the protease enzyme to discover a new part of the enzyme’s structure that would be vulnerable to chemical inhibition.
They found that before the protease assumes its doughnut shape, two ends have to bind together to close the circle. Where these two flaps join is the site that Carlson’s team chose to focus on.
Using their computer models, they developed a chemical inhibitor that was successful at stopping the two ends from joining and the enzyme from maturing into its final shape.
The chemical inhibitor they developed is too weak to work as a drug in the human body, but Carlson’s discovery does offer a potential new target for drug development.
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The facts are simple, and they are politically intimidating. There really are only two that matter. First, the study proved beyond doubt that the drug Tenofovir stops HIV infections to more than half of the abusers who inject heroin, methamphetamine and other illicit drugs.
In Thailand, where a few cases of compulsory licensing in 2007 caused massive trade and diplomatic problems, Tenofovir is in a kind of legal limbo. While it has not been submitted for CL, neither has it
won a Thai patent, a step needed to legalize that 428,000 baht-per-patient cost.
The Tenofovir used in the field study with drug abusers was produced by the Government Pharmaceutical Organization (GPO). Despite a somewhat murky legal status, it is available at some pharmacies, hospitals etc.
In their discovery of a new way to inhibit formation of HIV’s protease enzyme, scientists may have identified a new drug target, according to new data published in the August 2008 issue of Biopolymers.
Protease is a doughnut-shaped enzyme involved in processing viral proteins and assembling them into new infectious viruses.
It is currently the target of a handful of drugs called protease inhibitors, all of which bind to and block the hole in the doughnut shape.
Heather Carlson, PhD, a professor of chemistry at the University of Michigan, and her colleagues used computer models of the protease enzyme to discover a new part of the enzyme’s structure that would be vulnerable to chemical inhibition.
They found that before the protease assumes its doughnut shape, two ends have to bind together to close the circle. Where these two flaps join is the site that Carlson’s team chose to focus on.
Using their computer models, they developed a chemical inhibitor that was successful at stopping the two ends from joining and the enzyme from maturing into its final shape.
The chemical inhibitor they developed is too weak to work as a drug in the human body, but Carlson’s discovery does offer a potential new target for drug development.
FOLLOW US: http://www.facebook.com/PlaneHealth twitter.com/PlaneHealth
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