The National Institute of General Medical Sciences (NIGMS), one of the National Institutes of Health, supports all research featured in this digest. Although only the lead scientists are named, coworkers and other collaborators also contributed to the findings.
In This Issue... September 15, 2011 |
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 Cool Image: Microscopic Mood RingsIvan Dmochowski • University of Pennsylvania These glowing capsules shine in stressful situations—literally. Called polymersomes, the round, man-made membranes are studded with light-emitting pigments called porphyrins. When the membrane encounters stress, like tension or heat, the pigments change their configuration. Since shape determines how the porphyrins absorb and release light, the pigments glow in different hues. Here, the stressed region is evident before the membrane ruptures. Only a few microns in size, these miniscule mood rings could be used in body scanning or injected into the bloodstream to provide clues about nearby stresses, such as arterial blockages. Image courtesy of Neha Kamat, University of Pennsylvania. Read more... |
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 DeCYPORing a Genetic DisorderBettie Sue Masters • University of Texas Health Science Center, San Antonio Scientists are a step closer to understanding, and possibly preventing, Antley-Bixler syndrome. Children born with the rare genetic disorder don't produce enough of an enzyme called CYPOR, resulting in facial deformities and ambiguous sex organs. New research has uncovered CYPOR's structure in humans, as well as the structural changes responsible for Antley-Bixler syndrome. The scientists showed in basic lab studies that the B-vitamin riboflavin can reverse the activity of defective CYPOR enzymes. Knowing CYPOR's structure will help them and others investigate riboflavin therapy's potential to prevent or treat the syndrome. Read
more... Caption: Human CYPOR with mutation sites marked for mild (green),
medium (blue) and severe (red) effects. Credit: Jung-Ja P. Kim.
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How Salmonella SucceedsMichael Ibba • Ohio State University The bacterium Salmonella infects about 1.4 million Americans every year, causing fevers, diarrhea and abdominal cramps. A new study shows that Salmonella uses a compound called beta lysine in its protein-modifying machinery, rather than the virtually universal alpha lysine. When genes coding for beta lysine were knocked out or replaced with the alpha version during experiments, Salmonella lost its ability to cause disease. This property makes the beta version, never before seen in protein synthesis, an attractive target for antibiotics. Read
more... Caption: Salmonella bacteria cause illness in humans. Credit: Janice Haney Carr and Bette Jensen, CDC. High res. image (JPG,
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 The Flip Side of SynthesisMartin Burke • University of Illinois One way to create complex molecules and medicines is to join simple chemical building blocks in repetitive reactions, like assembling Lego bricks. But until recently, this technique—iterative cross-coupling—has been limited to molecules with one type of polarity. Now chemists have developed a reverse-polarity version of the technique, opening doors to a whole new batch of building blocks. The approach helped the research team synthesize synechoxanthin, a powerful antioxidant potentially useful for human health. Read
more... Caption: A new technique helps build complex molecules. High res. image (JPG, 93KB) |
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Rise of the Virtual RatDaniel Beard • Medical College of Wisconsin At a new systems biology center in Milwaukee, lab rats are going virtual. Drawing on genetic data and tissue samples, researchers are creating computer models of how the rat cardiovascular system works in health and disease. The work will shed light on how genetics and environmental factors interact to cause disease, a question that has long puzzled scientists. The ultimate goal is to use genes to predict a rat's heart health, which could lead to a similar approach for predicting complex human health conditions like high blood pressure and heart failure. Read more... Caption: Virtual rats could help predict heart health. |
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