Lifeboat Foundation

Researchers are still optimistic about finding disease-altering medicines—just not anytime soon.

• By Karen Weintraub on July 18, 2019

For the past quarter century, scientists battled Alzheimer’s disease under a single guiding principle: that protein clumps—beta-amyloid—deposited outside sensitive brain cells gradually damage neuronal functions and trigger memory loss. The solution seems simple: remove junk amyloid, protect the brain.

They could be completely wrong.

Last month, Alzheimer’s disease defeated another promising near-market drug that tried to prevent or remove amyloid deposits, adding to the disease’s therapeutic “graveyard of dreams.” Although the drug removed toxic amyloid, the patients didn’t get better. The failure is once again spurring scientists to confront an uncomfortable truth: targeting amyloid clumps when patients already show memory symptoms doesn’t work. Wiping out soluble amyloid—fragments of proteins before they aggregate into junk—also dead ends.

One of the most dangerous but thankfully rare mosquitoborne diseases has been spotted again in Florida, state health officials say. According to a public advisory issued this month by the Florida Department of Health in Orange County, the Eastern equine encephalitis virus (EEEV) was found in the state. The virus is capable of causing severe brain damage that can kill up to a third of its human victims.

EEEV can be spread by several species of mosquitoes, including those that make their home along the warmer areas of the U.S. Though many people infected with EEEV either develop no or only flu-like symptoms, around 5 percent go on to experience serious brain swelling (the titular encephalitis). This swelling can then lead to headaches, drowsiness, convulsions, and coma, with death coming as quickly as two days after symptoms start. And even if you’re lucky enough to survive the experience, you’ll probably be left with lifelong neurological impairment.

Working with mouse and human tissue, Johns Hopkins Medicine researchers report new evidence that a protein pumped out of some—but not all—populations of “helper” cells in the brain, called astrocytes, plays a specific role in directing the formation of connections among neurons needed for learning and forming new memories.

Using mice genetically engineered and bred with fewer such connections, the researchers conducted proof-of-concept experiments that show they could deliver corrective proteins via nanoparticles to replace the missing protein needed for “road repairs” on the defective neural highway.

Since such connective networks are lost or damaged by neurodegenerative diseases such as Alzheimer’s or certain types of intellectual disability, such as Norrie disease, the researchers say their findings advance efforts to regrow and repair the networks and potentially restore normal brain function.

In 2017, Facebook announced that it wanted to create a headband that would let people type at a speed of 100 words per minute, just by thinking.

Now, a little over two years later, the social media giant is revealing that it has been financing extensive university research on human volunteers.

Today, some of that research was described in a scientific paper from the University of California, San Francisco, where researchers have been developing “speech decoders” able to determine what people are trying to say from their brain signals.

In about 100 years, theoretical physicist Michio Kaku believes we’ll explore the universe as pure consciousness — traveling at the speed of light, looking at asteroids, comets, meteors, and eventually the stars. “All of this within the laws of physics,” he says.

Researchers from the Beijing Institute of Brain Disorders have discovered a new method of using exosomes to deliver aptamers that prevent the accumulation of α-synuclein aggregates, which are the cause of Parkinson’s disease [1].

α-Synuclein Aggregates

Like Alzheimer’s, Parkinson’s disease is characterized by protein aggregation caused by a loss of proteostasis, one of the hallmarks of aging. In order for the brain to function properly, non-aggregated α-synuclein proteins are needed in order to facilitate the release of dopamine, a neurotransmitter, in nerve cell synapses. α-synuclein only becomes a problem when proteostasis fails and the proteins misfold, aggregate, and accumulate.

Scientists at work in laboratory. Photo: Public domain via Wikicommons.

CTech – When chemistry Nobel laureate Michael Levitt met his wife two years ago, he didn’t know it would lead to a wonderful friendship with a young Israeli scientist. When Israeli scientist Shahar Barbash decided to found a startup with the aim of cutting down the time needed to develop new medicine, he didn’t know that a friend’s wedding would help him score a meeting with a man many want to meet but few do. But Levitt’s wife is an old friend of Barbash’s parents, and the rest, as they say, is history.

One of the joys of being an old scientist is to encourage extraordinary young ones, Levitt, an American-British-Israeli biophysicist and a professor at Stanford University since 1987, said in a recent interview with Calcalist. He might have met Barbash because his wife knew his family, but that is not enough to make him go into business with someone, Levitt said. “I got on board because his vision excited me, even though I thought it would be very hard to realize.”