The Food and Drug Administration on Wednesday announced meeting dates for advisors to discuss lifting restrictions on 12 unproven peptides that the agency deemed to pose significant safety risks in 2023. The meetings are scheduled for two days in July, with another in February 2027.

The scheduled meetings do not appear to be accompanied by any significant new safety or efficacy data for FDA advisors to discuss. Rather, the FDA is being pushed to ease restrictions on these peptides at the behest of anti-vaccine Health Secretary Robert F. Kennedy Jr., who has described himself as a "big fan" of the unproven drugs.

Peptide drugs are simply those made of short chains of amino acids linked by peptide bonds. FDA-approved peptide drugs include insulin for diabetes and GLP-1 drugs for obesity. But online, peptides typically refer to unproven drugs, often given by injection, that are peddled without evidence as treating various conditions, reversing aging, and improving appearance. This category has seen a boom in popularity among wellness influencers, including Kennedy and many of his allies.

Peptide proponents

Kennedy, who has no background in science or medicine, has repeatedly championed peptides and touted his use of the unproven drugs, which are currently available on the black and gray markets. In a February appearance on Joe Rogan's podcast, Kennedy said he used them to treat injuries to "really good effect." He has also previously vowed to end the FDA's "war on peptides."

In a social media post on Wednesday, Kennedy built on that rhetoric, saying that with the agency's scheduled meetings, "we took long-overdue action to restore science, accountability, and the rule of law."

He claimed that in the meetings, "independent experts will rigorously evaluate each substance on its scientific merits using full clinical, pharmacological, and safety evidence."

But outside experts are highly skeptical of the meetings. Currently, the FDA advisory panel that will review the drugs—the Pharmacy Compounding Advisory Committee (PCAC)—only has three voting members and one industry representative. There are six vacancies, including the chairperson.

Outside experts and watchdogs suspect that before the first meeting in July, Kennedy will work to stack the advisory board with questionably qualified allies who will come with a predetermined decision to ease access to the drugs—no rigorous scientific evaluation needed. A similar scenario has played out at the Centers for Disease Control and Prevention, where Kennedy stacked a key vaccine advisory committee with allies who then rammed through recommendations in line with Kennedy's anti-vaccine agenda. Those advisors made recommendations that were not supported by scientific evidence and, in some cases, directly conflicted with the data.

Risky peptides

Specifically, the PCAC will consider moving the 12 peptides back onto a list of drugs that compounding pharmacies can make for human use. Compounding pharmacies are those intended to make custom or specialized formulations of medications for patients. In 2023, the FDA removed 19 peptides from that list, finding they posed significant safety risks. The agency explained its concerns for each of the drugs individually.

"There is no credible reason to believe that peptides that were deemed unproven or unsafe in 2023 are miraculously safe and effective in 2026," Robert Steinbrook, Health Research Group director at consumer watchdog Public Citizen, said in a statement. "These peptides should go through the standard FDA approval process for new drugs, not a more lenient alternate pathway that defeats the reason the agency exists in the first place. If there were convincing safety and effectiveness data, the findings would already be widely known."

On July 23 and 24, FDA advisors will review seven of the 12 peptides, including BPC-157,KPV, TB-500 (a fragment of thymosin beta-4), MOTs-C, Emideltide (DSIP), Semax (heptapeptide), and Epitalon. In February 2027, the group will review the remaining five: Cathelicidin (LL-37), GHK-Cu, Dihexa-acetate, Melanotan II, and Mechano Growth Factor, Pegylated (PEG-MGF).

These peptides have no proven uses. The FDA lists uses for the first seven, but they don't necessarily match how people are using them or marketing them online. For instance, BPC-157, which was first isolated from gastric juices, is a popular peptide used to promote tissue repair, particularly for athletic injuries. The FDA lists its use as treating ulcerative colitis.

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A Chinese ship has tested a new device capable of slicing through submarine data cables thousands of meters beneath the ocean surface. That demonstration may exacerbate security concerns over a spate of suspected sabotage incidents targeting undersea communications and power cables from the Baltic Sea to the Pacific Ocean.

The trial took place at a depth of 11,483 feet (3,500 meters) during a deep-sea science expedition involving the Chinese research ship named Haiyang Dizhi 2, according to the South China Morning Post. That ship is equipped with a 150-ton crane, a 10-kilometer fiber optic winch, and a helicopter landing platform. It has shown the capability to deploy deep-sea remotely operated vehicles in previous missions.

The South China Morning Post cited a report in the China Science Daily, an official, Chinese-language news publication run by the Chinese Academy of Sciences. The latter claimed that “the sea trial has bridged the ‘last mile’ from deep-sea equipment development to engineering application.”

This is the latest of multiple dual-use technologies for cutting undersea cables developed by Chinese military and civilian organizations over the years. Previous examples include People’s Liberation Army naval organizations filing patents for cable-cutting and retrieval tools, as well as Lishui University filing a patent for a cable-cutting device that could be towed behind a vessel for emergency use, according to the Jamestown Foundation think tank based in Washington, DC. Such technology also debuts at a time when a growing number of Chinese-registered ships have been involved in damaging subsea data cables and even pipelines across the world.

How it works beneath the waves

The cable-cutting technology is reportedly designed to cut subsea cables at maximum depths of 13,123 feet (4,000 meters). Its design was first published in the Chinese-language journal Mechanical Engineer in 2025 and attributed to researchers at the China Ship Scientific Research Center and the State Key Laboratory of Deep-sea Manned Vehicles.

The submarine cable-cutting technology relies on an electro-hydrostatic actuator consisting of a hydraulic pump, an electric motor, and a control unit. That compact device enables a diamond-coated grinding wheel to exert enough force to cut through undersea cables armored with layers of steel, rubber, and polymer, according to the South China Morning Post’s earlier reporting from 2025. It’s also small enough to fit aboard one of China’s many underwater remotely operated vehicles.

The Chinese “display of deep-sea cable-cutting technology” represented a “show of strength,” said Wendy Chang, an analyst at the Mercator Institute for China Studies in Germany, when the technology initially came to light in 2025.

“From continuing to deny its involvement in shadowy operations involving doctored anchors to unveiling equipment to cut fortified cables, China is sending mixed messages about its role in global submarine infrastructure,” said Chang. “It wants to be a player in its construction and operation—but also wants the world to know that it has the capability to disrupt critical infrastructure if necessary.”

China is not alone in having the technological capability to access and potentially cut undersea cables. During the Cold War, the US Navy used a specially modified submarine and divers to secretly tap Soviet naval communications running through an undersea cable in the Sea of Okhotsk. Both the US and Russia continue to operate nuclear submarines and survey ships equipped with robotic submersibles that could access undersea cables. Some of the latest incidents of accidental or suspected sabotage damage to undersea cables have even simply involved ships dragging their anchors across the seafloor.

Dual-use ambiguity raises sabotage concerns

The Chinese researchers have insisted that the cable-cutting technology is intended for civilian purposes involving “marine resource development.” But the South China Morning Post has speculated that the tool could pose a threat to the fiber-optic cables linking to Pacific islands such as Guam, the US overseas territory that hosts several military bases.

Such a tool would also exacerbate Chinese military pressure on the self-governing democracy of Taiwan, which relies on 24 major cables for its global connectivity. Taiwan has faced a series of suspected undersea cable sabotage incidents involving Chinese-owned ships as part of a broader pressure campaign by Chinese military and maritime militia vessels, which have conducted multiple exercises in the waters near Taiwan.

Chinese-flagged cargo ships have even damaged undersea data cables and gas pipelines in the Baltic Sea at least twice in October 2023 and November 2024, affecting European countries such as Germany, Finland, Lithuania, Estonia, and Sweden. Chinese officials described those incidents as accidents.

Given the broader pattern of suspected sabotage incidents, it’s not hard to imagine some cause for concern in the newest cable-cutting tool’s dual-use capabilities. It’s also a reminder of the growing vulnerability of the Internet’s physical backbone, which consists of more than 1.5 million kilometers of submarine cables that stretch across oceans and connect continents.

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At the end of last month, a scientific journal pulled a research paper on Alzheimer's disease.

The retraction came from Neurobiology of Aging, which removed a 2011 paper claiming to show that a version of a protein called amyloid-β was responsible for memory loss in Alzheimer's disease. On its own, that might not seem notable; bad papers can make it through peer review and are only caught after publication.

But this wasn't an isolated case. Over the past few years, multiple studies arguing that amyloid-β is the central driver of Alzheimer's disease have been retracted. Some scientists have even been indicted for fraud over the issue. All the while, none of the drugs targeting this protein and its pathway have had any real clinical effect.

Why does this keep happening?

Plaques and tangles

The medical condition we currently call Alzheimer's disease was first identified in 1906, after a neuropathologist named Alois Alzheimer examined brain tissue from the autopsy of Auguste Deter, a dementia patient he had been treating. Deter was just 55 when she died, much younger than most dementia patients. Alzheimer noted that her brain tissue contained plaques, which had previously been seen in other dementia patients, as well as tangles of nerve fibers, which had not.

For the next 80 years, that was about as much as we knew about this condition that robs sufferers of their memories, skills, and personalities. And until very recently, it was only possible to diagnose it post-mortem by examining the brain for those plaques and tangles. The advent of PET scanners and the discovery of biomarkers in blood have changed that.

It wasn't until 1984 that we identified amyloid-β accumulating in the plaques of people with Alzheimer's. Scientists weren't really sure what amyloid-β did, but another study found plenty of it in the brains of people with Down syndrome, who often suffer from dementia later in life. In fact, the gene that encodes amyloid-β—or more accurately, for an upstream molecule called amyloid precursor protein—is found on chromosome 21, and the signature of Down syndrome is an extra copy of that. Raising suspicions further, in 1987, patients with a familial case of Alzheimer's were found to have a mutation in their amyloid protein precursor gene.

Something was causing amyloid-β to be cut off from its precursor, then clump together, in people with dementia. If only we could stop it from aggregating or remove the aggregates from the brain, we could stop the disease, the conventional wisdom held.

In 2006, this idea looked even better, as a paper was published in Nature showing that memory loss was associated with a specific form of amyloid-β buildup outside of neurons.

Stay on target

A potential therapeutic target gave scientists something to aim for. As with so many other poorly understood, complex diseases, they set about studying it in mice. But like so many of those other complex diseases that afflict humans, mice don't naturally get Alzheimer's. They do if you insert a mutated copy of the human APP gene into their genome, however. Armed with this early mouse model, scientists got to work.

In 1999, Elan Pharmaceuticals created a vaccine to a particular part of amyloid-β and then showed that mice would clear plaques from their brains after treatment with the vaccine. Better still, it worked whether the vaccine was given to very young mice, before the plaques could form, or to older mice where the plaques were already present.

Vaccines work by prompting the body to produce antibodies against whatever the vaccine recognizes. So a few years later, Elan went on to show that anti-amyloid antibodies also cleared plaques in the transgenic mice's brains when given directly.

But there's many a slip between mouse and man. Elan tried its vaccine in human patients suffering mild to moderate Alzheimer's disease but had to suspend the trial of 360 patients after a number developed brain inflammation. While Elan's vaccine didn't go anywhere, other pharmaceutical companies and biotechs were still on the case.

Trial after trial failed to arrest or reverse the disease, no matter the approach. Targeting different parts of the amyloid-β pathway also created side effects aplenty, some of them life-threatening or fatal. Regardless, amyloid-β remained the preferred target. Eventually, in 2021, the Food and Drug Administration approved an antibody called aducanumab, made by Biogen.

To call the approval controversial would be an understatement. Aducanumab had failed not one but two large double-blind, placebo-controlled phase III trials in 2019. Eventually, its makers scoured the data sets a little more, claiming to find a small reduction in amyloid-β plaque size and a small cognitive improvement in a particular group of participants.

Many scientists were outraged by the approval, and their outrage looked justified once we saw how the drug would be marketed: with a cognitive test that no one could pass. A congressional inquiry into aducanumab's approval found it was "rife with irregularities." But at $65,000 per patient per year, the drug represented a potential $18 billion-a-year revenue stream for Biogen.

Aducanumab was approved by the FDA in June 2021. But by early July, the regulator had already narrowed the set of people it would allow the drug to be given to, restricting it to just patients with a mild form of the disease. Biogen ended up losing money on it and removed the drug from the market in January 2024.

But only so it could concentrate on another amyloid-β-targeting antibody, this one developed with a biotech company called Eisai. This therapy, called lecanemab, was half the price of aducanumab, at $26,500 per year, and it got the nod from the FDA in 2023. There were plenty of questions about the approval because, yet again, there was very little data indicating that patients were getting any better. And there were still nasty side effects; three patients died from brain swelling and hemorrhaging.

Another antibody targeting amyloid-β, called donanemab, made headlines in 2023 when its maker, Eli Lilly, published trial data that claimed to slow the progression of the disease "by about 35 percent in the early stages." Again, this came with the risk of severe side effects like brain swelling and bleeding. Those side effects may have been the only way to tell someone was on the drug, given that it provided extremely mild cognitive benefits.

Surely we've had some other ideas?

We're now more than 40 years on from the identification of amyloid-β as the bad stuff in plaques and 30 years from being able to clear amyloid-β from the brains of mice (and, more recently, humans). Yet doing that is more likely to make an Alzheimer's patient's brain bleed than it is to restore cognitive function or even meaningfully slow its decline. But it's not like we haven't had other ideas.

Take inflammation, for instance. Brains aren't just made of neurons; they're surrounded by glial cells, some of which envelop the neuronal junctions. Some of these glia are similar in ways to macrophages, a kind of immune cell that goes a little haywire in heart disease and some other conditions. In 2008, a small-scale study showed that the arthritis drug etanercept, which inhibits an inflammatory cytokine called TNF-α, caused a rapid improvement in cognitive function for Alzheimer's patients.

The only hitch? The drug needed to be infused directly into the spinal column. A larger trial that used etanercept injections under the skin didn't run into any of the horrible side effects of the amyloid-β antibodies, but it also failed to show any real clinical benefit.

To others in the scientific community, the trigger for that inflammation is likely to be infection. Our immune system uses cytokines like TNF-α to fight infections, in addition to other chemicals like peroxynitrite, which causes oxidative stress, all of which is associated with inflammation.

Neuropathologists have identified viral infections in plaques, and a group from Tufts recently proposed a mechanism by which herpes simplex virus-1 could be driving the disease. But many other viruses have also been implicated; data-mining samples from biobanks in the UK and Finland found infections from several different viruses were associated with an increased risk of Alzheimer's disease (as well as other neurological disorders), with the most striking correlation being viral encephalitis.

Even influenza infection was associated with a five-fold increase in the risk of developing Alzheimer's. But again, the data is equivocal and a little confusing. In that study, the risk of developing Alzheimer's was greatest at one year after infection and then decreased over time. But we know that the disease takes decades to progress.

Bacterial infections have also seen scrutiny. Porphyromonas gingivalis is an anaerobic bacterium that's one of the main culprits of gum disease, and it has been linked to a range of common diseases, including things like atherosclerosis and—you guessed it—Alzheimer's. The idea is that p. gingivalis enters the bloodstream through abrasions in the mouth and then reaches the brain; the response causes the plaques and tangles to form.

Still other research has suggested a role for our gut microbiome, the vast collection of microbes that help us digest food—more recently, we've discovered they do so, so much more. Here, tantalizingly, there are other hints of therapeutic targets. For example, foods that reduce inflammation, such as those high in fiber or omega-3 fatty acids, may be neuroprotective, in addition to being good for your heart. And a variant of the APOE4 gene that results in high levels of LDL cholesterol is also associated with an increased risk of Alzheimer's.

The problem with any of these hypotheses is that many, many more people will be infected with a virus or bacteria that has been implicated in Alzheimer's than will ever develop the disease. Two-thirds of people under 50 have HSV-1, for example, and they won't all get Alzheimer's. The same goes for people with gum disease or an influenza infection. Perhaps the disease requires multiple different pathogens to be sparked?

More likely, each of these can insult the brain and trigger plaque formation, but only in combination with other factors. Recently, a role for lithium deficiency has looked rather compelling.

The Amyloid Mafia

We would almost certainly know a lot more about those other potential causes had it not been for the so-called Amyloid Mafia. Scientists aren't immune to groupthink, and the people responsible for deciding who got research grants and who didn't have not been at all receptive to proposals that investigate non-amyloid mechanisms.

"You were just lucky when you weren’t beaten up by the amyloid-β or tau people if you would mention immunology," said Michael Heneka, a neuroinflammation specialist interviewed by Nature in 2023. (Tau is another Alzheimer ’s-associated protein.)

Speaking to American Public Media, the former director of Alzheimer's research at the National Institute of Aging said, "It became gradually an infallible belief system. So everybody felt obligated to pay homage to the idea without questioning. And that's not very healthy for science when scientists... accept an idea as infallible. That's when you run into problems."

To make matters worse, it turned out that much of that confidence in amyloid-β as the one true cause was built on fake data.

That landmark 2006 Nature paper that claimed to show that a specific form of amyloid-β was the culprit causing the disease? It was retracted in 2024 after it emerged that the authors had faked some of the data, copy-pasting images of protein detections. In another case, a scientist at City University of New York was indicted last year for falsifying data that helped support the ideas behind an Alzheimer's drug being developed by Cassava Sciences. (For a more comprehensive look at the Amyloid Mafia, check out Charles Pillar's work.) Sadly, this kind of scientific misconduct is more common than we'd like and can be hard to detect before publication.

Those FDA drug approvals have also been tainted. In addition to the aforementioned congressional investigation that found irregularities, the head of FDA's neuroscience office was forced to step down in 2023 after it was found that he had an inappropriately close relationship with Biogen.

Despite this litany of clinical failures and research misconduct, it would be a stretch to say that the amyloid hypothesis is dead. Only one of the five FDA-approved therapies is independent of the amyloid pathway, and while work is conducted on other areas, amyloid-β research remains the lion's share.

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So you thought you'd just read that webpage and then go back to the previous page? A bold assumption. All too often, clicking the back button in your browser doesn't actually take you back. It's called back button hijacking, and Google has thus far tolerated it. That ends in June, when the company will designate it a "malicious practice," and any site continuing to do it will face consequences.

Back button hijacking is a way of wringing more pageviews out of visitors. It's common on sites that live and die on search traffic. You may end up on a page because it looks like something you want, but instead of letting you leave the domain, it manipulates your page history to insert something else when you click back.

The phantom page is usually a collection of additional content suggestions or a pop-up that tries to eke out a few more clicks from each visitor. Some sites get a little more creative with it, though. For example, LinkedIn has a nasty habit of sending you "back" to the social feed after you land on a link to a profile or job posting.

Google says the back button should always do what you expect it to do—go back. Anything else amounts to a deceptive user experience that can discourage users from visiting unfamiliar pages in the future. The company isn't inventing a new rule to address this behavior, which is apparently on the rise. Google will simply be more broadly enforcing the malicious practices policy, which says in part:

Malicious practices create a mismatch between user expectations and the actual outcome, leading to a negative and deceptive user experience, or compromised user security or privacy.

Sites that have been using back button hijacking are now under the gun to end the practice. Starting on June 15, 2026, sites using back button hijacking could be hit with either automated or manual anti-spam actions. That can result in a much lower page rank in search, which is a problem for sites that have traditionally relied on search traffic to stay afloat.

Google says that any site that uses back button hijacking should spend the next two months eliminating the practice. The early warning ensures they'll have a chance to get it done. While some websites have designed their own systems to do this, others have back button hijacking as a consequence of a third-party library or advertising stack. Whatever the origin of the hijack, sites will want to get it sorted out before the deadline to avoid a spam designation.

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A Chicago concert superfan Aadam Jacobs who has recorded more than 10,000 shows since the 1980s is working with Internet Archive volunteers to digitize the collection before the cassettes deteriorate. "So far, about 2,500 of these tapes have been posted on the Internet Archive, including some rare gems like a Nirvana performance from 1989," reports TechCrunch. From the report: For many of these recordings, Jacobs was using pretty mediocre equipment, but the volunteer audio engineers working with the Internet Archive have made these tapes sound great. One volunteer, Brian Emerick, drives to Jacobs' house once a month to pick up more boxes of tapes -- he has to use anachronistic cassette decks to play the tapes, which get converted into digital files. From there, other volunteers clean up, organize, and label the recordings, even tracking down song names from forgotten punk bands. The archive is available here.

Read more of this story at Slashdot.

Last time, we looked at adding or removing a handle from an active Wait­For­Multiple­Objects, and we developed an asynchronous mechanism that requests that the changes be made soon. But asynchronous add/remove can be a problem bcause you might remove a handle, clean up the things that the handle was dependent upon, but then receive a notification that the handle you removed has been signaled, even though you already cleaned up the things the handle depended on.

What we can do is wait for the waiting thread to acknowledge the operation.

_Guarded_by_(desiredMutex) DWORD desiredCounter = 1;
DWORD activeCounter = 0;

void wait_until_active(DWORD value)
{
    DWORD current = activeCounter;
    while (static_cast<int>(current - value) < 0) {
        WaitOnAddress(&activeCounter, &current,
                      sizeof(activeCounter), INFINITE);
        current = activeCounter;
    }
}

The wait_until_active function waits until the value of active­Counter is at least as large as value. We do this by subtracting the two values, to avoid wraparound problems.¹ The comparison takes advantage of the guarantee in C++20 that conversion from an unsigned integer to a signed integer converts to the value that is numerically equal modulo 2ⁿ where n is the number of bits in the destination. (Prior to C++20, the result was implementation-defined, but in practice all modern implementations did what C++20 mandates.)²

You can also use std::atomic:

_Guarded_by_(desiredMutex) DWORD desiredCounter = 1;
std::atomic<DWORD> activeCounter;

void wait_until_active(DWORD value)
{
    DWORD current = activeCounter;
    while (static_cast<int>(current - value) < 0) {
        activeCounter.wait(current);
        current = activeCounter;
    }
}

As before, the background thread manipulates the desiredHandles and desiredActions, then signals the waiting thread to wake up and process the changes. But this time, the background thread blocks until the waiting thread acknowledges the changes.

// Warning: For expository purposes. Almost no error checking.
void waiting_thread()
{
    bool update = true;
    std::vector<wil::unique_handle> handles;
    std::vector<std::function<void()>> actions;

    while (true)
    {
        if (std::exchange(update, false)) {
            std::lock_guard guard(desiredMutex);

            handles.clear();
            handles.reserve(desiredHandles.size() + 1);
            std::transform(desiredHandles.begin(), desiredHandles.end(),
                std::back_inserter(handles),
                [](auto&& h) { return duplicate_handle(h.get()); });
            // Add the bonus "changed" handle
            handles.emplace_back(duplicate_handle(changed.get()));

            actions = desiredActions;

            if (activeCounter != desiredCounter) {
                activeCounter = desiredCounter;   
                WakeByAddressAll(&activeCounter); 
            }
        }

        auto count = static_cast<DWORD>(handles.size());
                        
        auto result = WaitForMultipleObjects(count,
                        handles.data()->get(), FALSE, INFINITE);
        auto index = result - WAIT_OBJECT_0;
        if (index == count - 1) {
            // the list changed. Loop back to update.
            update = true;
            continue;
        } else if (index < count - 1) {
            actions[index]();
        } else {
            // deal with unexpected result
        }
    }
}

void change_handle_list()
{
    DWORD value;
    {
        std::lock_guard guard(desiredMutex);
        ⟦ make changes to desiredHandles and desiredActions ⟧
        value = ++desiredCounter;
        SetEvent(changed.get());
    }
    wait_until_active(value);
}

The pattern is that after the background thread makes the desired changes, they increment the desiredCounter and signal the event. It’s okay if multiple threads make changes before the waiting thread wakes up. The changes simply accumulate, and the event just stays signaled. Each background thread then waits for the waiting thread to process the change.

On the waiting side, we process changes as usual, but we also publish our current change counter if it has changed, to let the background threads know that we made some progress. Eventually, we will make enough progress that all of the pending changes have been processed, and the last ackground thread will be released from wait_until_active.

¹ You’ll run into problems if the counter increments 2 billion times without the worker thread noticing. At a thousand increments per second, that’ll last you a month. I figure that if you have a worker thread that is unresponsible for that long, then you have bigger problems. But you can avoid even that problem by switching to a 64-bit integer, so that the overflow won’t happen before the sun is expected to turn into a red giant.

² The holdouts would be compilers for systems that are not two’s-complement.

The post How do you add or remove a handle from an active <CODE>Wait­For­Multiple­Objects</CODE>?, part 2 appeared first on The Old New Thing.