Imagine a world without AIDS

The coming of age of Peptide T

Almost fifteen years ago I gave a presentation to my son’s elementary school about Dr. Michael Ruff’s and my discovery of peptide T and its application as an AIDS treatment. The presentation was prompted by my son Brandon’s brag to his friends, “My mother’s found the cure for AIDS.” Cringing over this announcement and a nine-year-old’s vision, I complied with the teacher’s request to come explain our NIH (National Institutes of Health) research to his fifth graders.

Kurt Vonnegut once said that the most complicated idea in the world - if you truly understand it yourself - should be easily explained to an eleven year old. Back then I didn’t really understand how the AIDS virus worked—but it was still the early years of the epidemic, before the term global pandemic was being used to describe AIDS. It was also before scientists had fully worked out how the viruses get into cells, and less than a decade since the virus that causes it had been isolated by American and French scientists.

The smart nine-year-olds easily grasped the idea that the virus grabs onto the receptor sites on the cell’s surface, like a lock in a key. They also easily “got” the way peptide T sits in the receptor and blocks the virus from entering and infecting cells.

Today, peptide T is more relevant than ever, as AIDS has rapidly spread throughout the world, becoming the most deadly infectious disease in history infecting over 30 million people, who will eventually die of the disease. The statistics are beyond depressing—a disease that was first noticed in the gay community is now a heterosexually transferred disease found mostly in women and children. Nearly two thousand AIDS orphans die every single day somewhere in the world. In some towns in South Africa , for example, half of the women are infected.

Despite these facts, today I am remarkably upbeat and excited about the prospect of ridding the world of the scourge of AIDS, for the latest scientific progress is now close to a vaccine to eradicate this disease. I think it’s as important for people to know the background of the science involved and how the vaccine works as it is to have the final little vial with the vaccine itself available.

As a graduate student, I figured out how to measure opiate receptors, the places on cells

where heroin, morphine, methadone, etc first bind and act. This led to the discovery of endorphins, the brain’s —and body’s—own morphine, peptides which suppress pain and produce euphoria, one of hundreds of kinds of molecules of emotion that I have written about in my research and popular books. Molecules of Emotion LINK

Now, a peptide is simply a short chain of two or more amino acids. Endorphins have between five and 31 amino acids. Insulin has 51. Proteins are enormous peptides with hundreds of amino acids. The envelope protein of HIV, the AIDS virus, which covers its surface and allows it to bind to its receptors has about 600 amino acids. I say “about” because the virus is mutating and different strains vary. AIDS researchers know the precise chemical formula or sequence of amino acids not just in the envelope protein, but every piece of the virus.

Peptide sequences are much like email addresses – one character wrong, too many or too few and the email will not be delivered. Peptide T is a string of exactly eight amino acids, an “octapeptide” that blocks the virus from entering cells because it is the attachment sequence derived from the virus itself. It is the address on the envelope that insures the viral package gets delivered.

Early in AIDS research when the sequence of the virus had just been discovered, people hoped to find such a short piece, but mistakenly ruled out even the idea of a short piece working after making tens of peptides, 20 amino acids long, that covered the entire envelope sequence and finding that none of them blocked binding or infectivity. Peptide T was dismissed because that approach had been “ruled out” by expert virologists who weren’t aware of the finer, more esoteric points of peptides! Also, peptide T was discovered years before scientists had worked out the co-receptors that the virus uses—in early experiments researchers could not find the very potent claimed peptide T effects because they were working with a virus that used a different, less important, receptor. Also, it took years to learn how to store peptide T to retain its potency.

Today all that has changed. AIDS researchers and government officials are joining together to test a peptide T-based vaccine that in rabbits appears to elicit antibodies that block strains of viruses from all over the word, the so- called “broadly reactive neutralizing antibodies” that have been the Holy Grail of research to find an AIDS vaccine. Like the search for the Holy Grail, it has proved so hard that many have decided it’s impossible. That’s why all vaccines to date are based on the entire big complicated structure of the envelope protein, even though these don’t give rise to neutralizing antibodies. Still, it is so challenging to do vaccine studies in the parts of the world where AIDS is spreading swiftly, that it is important that experimental vaccine work continue to prime the pump. The infrastructure that will eventually prove the efficacy of a “broad spectrum” vaccine that will block all people from catching the virus, and even treat people who already have the virus, must continue to function.

So now, fifteen years from that long-ago elementary school lecture, I am finally catching up to my son’s vision and imagining a world without AIDS. Scientists are now working closely together to come behind the promising new peptide T vaccine data that we will present in March at the Global AIDS Vaccine Conference in Vancouver, Canada. I see myself learning from the vaccinologists who know how to attach our viral peptides to substances that will create a safe and effective vaccine. I see us all filled with gratitude in the present moment, forgetting our missteps of the past, grateful that the scientific method will give rise to a cure for AIDS, I believe, within a mere three decades from the isolation and sequencing of the virus. The first human tests with the brilliant NIH-funded infrastructure in place could begin within two to three years. I pray progress continues swiftly.

Candace Pert, PhD is a former NIH section chief, Georgetown University Medical School professor, and currently the founder and Scientific Director of The Institute for New Medicine www.TINM.org [1]. Dr. Pert is the author of Molecules of Emotion. The new Hay House book Everything You Need To Know to Feel Go(o)d tells of her own personal journey toward the healing necessary to bring forth her AIDS discoveries.

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New Weapon May Help Flush Stealth Stashes of HIV in Cells

From a Georgetown University Medical Center press release

Washington, D.C. – The first human study to assess antiviral and immune effects of the experimental therapy, called Peptide T® [occurred in 2003]. Although a small trial, it yielded statistically significant data on Peptide T’s ability to purify cells housing hidden HIV virus without any harmful side effects. This flushing mechanism gives promise to a new class of viral entry inhibitor drugs as a complement or perhaps even an alternative to the popular but costlier and complicated “highly active anti-retroviral therapies” (HAART) drug regimens.

“Every person in the study took Peptide T, and in each one of them, we observed quite a remarkable phenomenon – their white blood cell reservoirs of virus plummeted, some to undetectable levels,” said Candace Pert, PhD, professor of physiology, co-discoverer of Peptide T, and lead Georgetown investigator of this study. “We’ve come a long way and undoubtedly have a ways to go, but the way Peptide T stirred the immune system and flushed the HIV cellular reservoirs is very encouraging to me.”

Conceptually, Peptide T could play a valuable role in the fight against HIV. While current anti-retroviral drug cocktails successfully kill active, replicating HIV, the virus also has a frustrating ability to hide silently in cells for an indeterminate time period. A formidable foe, these hidden sources of virus may instantly be triggered and cause the virus to suddenly and aggressively kick start, beginning the chain of events that leads to the progression toward HIV/AIDS.

People with HIV currently remain on HAART drugs long after their virus plasma levels dip to undetectable levels simply because doctors know that hidden stores of virus hide within cells, looking for an opportunistic gateway to open and allow them to act up. If Peptide T one day conclusively flushes these hidden viral components out of the system for good, HIV-positive people could cease taking the costly drug cocktails they currently take as a defensive measure

Drs. Pert and Ruff discovered Peptide T -- a synthetic compound of amino acids -- while Pert was serving as the chief of the brain biochemistry section at the National Institute of Mental Health in the late 1980s. It works by blocking HIV from entering cells by binding to the CCR5 receptors the virus uses to enter and infect cells. This is a much different action that antivirals that work directly on HIV or infected cells.

Earlier studies conducted on Peptide T sponsored by the National Institutes of Health have reported neurocognitive and brain imaging benefits of Peptide T in people with AIDS. Importantly, all previous studies have demonstrated that there are no toxicities associated with Peptide T.