The science behind a favorite childhood activity, can a former party drug be the cure for depression and is CRISPR getting too big?
(Science Daily, 8/28/2018, New York University)
Nothing says summer like children outside blowing bubbles. But what exactly happens when you blow on a soap film to make a bubble? In a series of experiments replicating bubble blowing, NYU’s Applied Math Lab has discovered two ways in which bubbles can be made: one, by pushing with a steady but strong wind on a soap film through a circular wand, which causes it to grow into a bubble, and two, by pushing with a gentle wind on an already-inflated film in order to drive its further growth.
(TIME, 8/29/2018, Jamie Ducharme)
A new study suggests that ketamine, an increasingly popular treatment for depression, has something in common with drugs like fentanyl and oxycodone. The small study found evidence that ketamine’s effectiveness with depression, demonstrated in many small studies over the past decade, comes from its interaction with the brain’s opioid system. A Stanford University team reported their findings Wednesday in The American Journal of Psychiatry. Until now, most researchers have attributed ketamine’s success to its effect on the brain’s glutamate system, which is involved in learning and memory. The opioid system, in contrast, controls pain, reward and addictive behaviors. Ketamine is an anesthetic that is frequently given to children in the emergency room. It is also a popular but illicit party drug that can cause an out-of-body experience at high doses.
(Science Magazine, 8/30/2018, Jon Cohen)
CRISPR is the rock star tool of biology but is it getting too big for its own good? Researchers have devised a way to put CRISPR on a diet and still retain its core functions. Standard CRISPR methods have appropriated a DNA-snipping protein called SpCas9 from the Streptococcus pyogenes bacterium. Another CRISPR component guides the enzyme to targeted places on the genome. SpCas9 binds the DNA and its molecular scissors clip the double-stranded helix. But this lab darling, which has 1368 amino acids, is too chunky for many biomedical applications. So a team led by David Savage of the University of California, Berkeley, has devised a huge library of slimmer Cas9s using a “directed evolution” scheme. The technique uses two enzymes to systematically snip the DNA of the SpCas9 gene, pulling out chunks encoding different parts of the protein. Savage and colleagues then test those genetic sequences to see whether their resultant proteins still retain Cas9’s ability to bind to DNA targets. They then combine the ones that succeed, to add to the unique truncated options. So far, they have made half a million variants.
—-Compiled by Social Media Specialist Jillian Scola