Newsletter For June 1st

Obstacles that HIV antibodies face in blocking HIV infection
--from a Caltech press release dated 4/22/09

Twenty-five years after the AIDS epidemic spawned a worldwide search for an effective vaccine against HIV, progress in the field has been effectively stalled. A team of researchers from Caltech theorize that this is at least partially influenced by the fact that the body's natural HIV antibodies simply don't have a long enough reach to effectively neutralize the viruses they are meant to target.

Y-shaped antibodies are best at neutralizing viruses (blocking their entry into cells and preventing infection) when both arms of the Y are able to reach out and bind to their target proteins at more or less the same time. In the case of HIV, antibodies than can block infection target the proteins that stud the surface of the virus; the proteins stick out like many spikes from the viral membrane. But an antibody can only bind to two spikes at the same time if those spikes fall within its span -- the distance the antibody's structure allows it to stretch its two arms.

The authors of the study state that when both arms of an antibody are able to bind to a virus at the same time, there can be a hundred to a thousand-fold increase in the strength of the interaction, which can sometimes translate into an equally dramatic increase in its ability to neutralize an antigen.

Having good neutralizing antibodies is the hallmark of an effective vaccine and the above theory may demonstrate why HIV vaccines have so far failed.

Reported by Joshua Klein, graduate student at Caltech and first author of the paper at the online early edition of the Proceedings of the National Academy of Sciences (PNAS).
http://mr.caltech.edu/press_releases/13252


Identifying specific molecules that can block the means by which HIV spreads : A report from an international team based at Rice University, Houston, TX
--from the American Chemical Society's Journal of Chemical Information and Modeling. 5/24/09

Rice University's Andrew Barron and his group have identified specific molecules that could block the means by which the deadly virus spreads by taking away its ability to bind with other proteins. In a unique collaborative effort, research groups from five institutions -- two in Greece, one in Germany, one in Italy and the Texas team -- came together through e-mail contacts and conversations over many months, each working on differing facets of the problem. Not only have all the groups not met in person, but even more surprisingly, their research to date has been completely unfunded.

Using computer simulations, researchers tested more than 100 Carbon fullerene, or C-60, derivatives (originally developed for other purposes) to see if they could be used to inhibit a strain of the virus, HIV-1 PR, by attaching themselves to its binding pocket. Using simulations to narrow down a collection of fullerenes to find the good ones is the least time-consuming low-cost procedure for efficient, rational drug design. A long time ago, people noticed that C-60 fits perfectly into the hydrophobic pocket in HIV, and it has an inhibitory effect. It’s not particularly strong, but there is definitely a viable potential for studying and using this type of technology. The Schick Foundation especially lauds the group for their innovative research approach.
http://www.bio-medicine.org/biology-news-1/International-team-tracks-clues-to-HIV-8504-1


Breaking News from The Schick Foundation

The Schick Foundation may form a partnership with Power Organics of Shasta, California to study the effects of Blue Green Algae in prospective clinical trials.

The Schick Foundation is planning to launch a landmark pilot study looking at the effects of Blue Green Algae on HIV+ patients whose virus has been suppressed via ART for at least 6 months.

If you want to see our unique and ground-breaking protocols flourish and succeed, please contribute to The Peter Schick Foundation, 1223 Wilshire Blvd. #1007, Santa Monica CA 90403. Donations may also be made directly through our websites: www.schick-foundation.org and http://www.schickresearch.com/.