Notes from the Back Row: "Making Molecules"

"I grew up cooking, waiting tables, and doing dishes in the family diner in Chicago," says Jonas Peters. These days, as Caltech's Bren Professor of Chemistry, Peters is more an executive chef than a spatula jockey: he coordinates the menu and helps dream up the recipes for new molecules, but his students whip them up and wash the glassware. In his Watson Lecture on March 14, 2012, Peters leads a cook's tour of the art and science of chemistry. In his words, "What holds molecules together? How do we design one, plan the recipe, and know how well it came out?"

"The craft of making molecules hasn't changed that much" since the days of the alchemists, says Peters. "Take of cranium humanum as much as you please," he says, quoting a recipe from John French's The Art of Distillation, written in 1651. "Break it into small pieces, which put into a glass retort well luted [sealed airtight], with a large receiver well luted. Put a strong fire to it by degrees, continuing of it until you see no more fumes come forth, and you shall have a yellowish spirit, a red oil, and a volatile salt. Take this salt and the yellow spirit, and digest them by circulation two or three months in balneum [in a hot bath], and you shall have a most excellent spirit." While this extract is no longer the remedy of choice for dropsy—whatever that is—its method of preparation will be familiar to anyone who spent some time in the chem lab in high school. 

On the other hand, the theory behind making molecules has advanced considerably, allowing modern chemists to create very complex arrangements of atoms by design. Peters's own lab, for example, contributes to Caltech's Joint Center for Artificial Photosynthesis, an initiative to develop the technologies needed to run our civilization entirely on sunlight. We are still a long way from that happy dawn, but we are well beyond another piece of advice from alchemist John French, who counseled the uninitiated to "try not at first experiments of great cost or great difficulty, for it will be a great discouragement to you, and you will be very apt to mistake." At Caltech, notes Peters, "we have fantastic grad students and postdocs, so we can dive right in and do experiments of great difficulty knowing they can pull it off."

"Making Molecules" is available for download in HD from Caltech on iTunesU. (Episode 10)

 

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Doug Smith
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Zooming in on Single Cells

A Caltech chemist improves imaging technology with the help of an NIH award

Last fall, assistant professor of chemistry Long Cai received a New Innovator Award from the National Institutes of Health (NIH)—funding meant to both stimulate highly innovative research and support promising new investigators. Now, just nine months later, Cai has published the first results of his supported research.   

The New Innovator Award is one of the NIH Director's Awards, administered through the organization's Common Fund. The fund provides support for biomedical research deemed to be both innovative and risky.

Cai and his colleagues are working to use high-powered microscopy to help them better understand the genetic programs in individual cells. "We developed a new technique to show that super-resolution microscopy (SRM)—which is a cool, single-molecule-based technology that has been used to zoom in on structures and organelles in cells—can also be used to look at genetic information within a cell, like RNA and proteins," says Cai, who joined the Caltech faculty in 2010.

His paper, "Single-cell systems biology by super-resolution imaging and combinatorial labeling," is available as an advance online publication of the journal Nature Methods.

With the help of coauthor Eric Lubeck, a graduate student in biochemistry and molecular biophysics, Cai labeled individual mRNA molecules within a cell with distinct molecular barcodes. When the cell is imaged using SRM, the barcodes can be resolved and used to read the gene expression levels.   

"If you want to look at a genetic network, then you want to look at many of the individual genes at the same time—this is a way to allow you to do that in single cells," says Cai. "This technique may provide valuable information about rogue cells that are involved in cancer and other diseases, and look at gene expression in single cells within their native environments."

He says that the idea was sparked after a discussion with Barbara Wold, Bren Professor of Biology, about transcription regulation and new advances in single- molecule techniques. "It's really great to have ideas stimulated from an afternoon discussion over coffee," says Cai, "and this is part of what makes Caltech special." The project was started nearly three years ago, when Cai was a Beckman Fellow in the laboratory of Michael Elowitz, professor of biology and a Howard Hughes Medical Institute investigator. "Michael was very generous in letting me use his microscopes and lab to start the experiment," he says. "The NIH award helped us to finish the work when I set up my own lab."

Cai explains that their new method combines two existing technologies. In their proof-of-principle study, the duo was able to measure mRNA molecules in 32 genes simultaneously and within the same cell.   

"Now we're trying to show that it is possible to look at 100 genes at the same time," says Cai, who thinks it will be possible to measure thousands of genes concurrently. "It's just a matter of time."  

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Katie Neith
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Caltech Chemical Engineers Devise New Way to Split Water

Nontoxic, noncorrosive, "low-temperature" method makes use of wasted heat

PASADENA, Calif.—Providing a possible new route to hydrogen-gas production, researchers at the California Institute of Technology (Caltech) have devised a series of chemical reactions that allows them, for the first time, to split water in a nontoxic, noncorrosive way, at relatively low temperatures.

A research group led by Mark Davis, the Warren and Katharine Schlinger Professor of Chemical Engineering at Caltech, describes the new, four-reaction process in the early edition of the Proceedings of the National Academy of Sciences (PNAS).

Hydrogen is a coveted gas: industry uses it for everything from removing sulfur from crude oil to manufacturing vitamins. Since its combustion does not emit carbon dioxide into the atmosphere, there is some belief that it could even fuel a potential "hydrogen economy"—an energy-delivery system based entirely on this one gas. But since there is no abundant supply of hydrogen gas that can be simply tapped into, this lighter-than-air gas has to be mass-produced.

One way to make hydrogen is by using heat to split water, yielding pure hydrogen and oxygen. Known as thermochemical water splitting, this method is appealing because it can take advantage of excess heat given off by other processes. Thus far, it has been attempted in two ways: using two steps and taking advantage of high temperatures (above 1000°C) associated with solar collectors; or through multiple steps at "lower temperatures"—those below 1000°C—where, for example, the excess heat from nuclear reactors could drive the chemistry.

Davis is interested in this latter approach, which actually takes him back to his academic roots: his first paper as a graduate student dealt with a low-temperature water-splitting cycle, called the sulfur-iodine system, which has since been piloted for use around the world. Although that cycle operates at a maximum temperature of 850°C, it also produces a number of toxic and corrosive liquid intermediates that have to be dealt with. The cycle's high-temperature counterparts typically involve simpler reactions and solid intermediates—but there are very few processes that produce excess heat at such high temperatures.

"We wanted to combine the best of both worlds," Davis says. "We wanted to use solids, as they do in the high-temperature cycles, so we could avoid these toxicity and corrosion issues. But we also wanted to learn how to lower the temperature."

The first thing postdoctoral scholar and lead author Bingjun Xu and graduate student Yashodhan Bhawe did was to prove via thermodynamic arguments that a two-step, low-temperature cycle for water splitting will not be practical. "Nature's telling you 'No way,'" Davis says. "It was really a key point that told us we had to go away from looking for a two-step process, and that guidance directed us down another pathway that turned out to be quite fruitful."

The four-reaction cycle the team came up with begins with a manganese oxide and sodium carbonate, and is a completely closed system: the water that enters the system in the second step comes out completely converted into hydrogen and oxygen during each cycle. That's important because it means that none of the hydrogen or oxygen is lost, and the cycle can run over and over, splitting water into the two gases. In the current paper, the researchers ran their newly created cycle five times to show reproducibility. It will be needed to show that the cycle can run thousands of times in order to be practical. Experiments of this type are beyond the capabilities currently in the Davis lab.

"We're excited about this new cycle because the chemistry works, and it allows you to do real thermochemical water splitting with temperatures of 850°C without producing any of the halides or other types of corrosive acids that have been problems in the past," Davis says. Still, he is careful to point out that the implementation of the cycle as a functioning water-splitting system will require clever engineering. For example, for practical purposes, engineers will want some of the reactions to go faster, and they would also need to build processing reactors that have efficient-energy flows and recycling amongst the different stages of the cycle.

Going forward, the team plans to study further the chemistry of the cycle at the molecular level. They have already learned that shuttling sodium in and out of the manganese oxide is critical in lowering the operating temperature, but they want to know more about what exactly is happening during those steps. They hope that the enhanced understanding will allow them to devise cycles that could operate at even lower maximum temperatures.

Figuring out ways to decrease the operating temperatures is at the heart of Davis's interest in this project. "What we're trying to ask is, 'Where are the places around the world where people are just throwing away energy in the form of heat?'" he says. He speculates that there could be a day when water-splitting plants are able to run on the heat given off by a variety of manufacturing industries such as the steel- and aluminum-making industries and the petrochemicals industries, and by the more traditional power-generation industries. "The lower the temperature that we can use for driving these types of water-splitting processes," he says, "the more we can make use of energy that people are currently just wasting."

The PNAS paper, "Low-temperature, manganese oxide-based thermochemical water splitting cycle" is now online. The work was funded by a donation from Mr. and Mrs. Lewis W. van Amerongen.  

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Kimm Fesenmaier
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From the Ground Up

What's it like to build an entire research program from scratch? It's all about becoming part of a community, according to three brand-new professors: 

"It's very important to generate an environment where people help each other." —André Hoelz 

"I have two challenges getting started here. One is bringing in students and postdocs, and the other is fostering a connection between economics and computer science." —Katrina Ligett

"It is not traditionally a field Caltech has done. . . . So when I was looking at coming to Caltech, the idea of being 'the oceanographer' was an exciting prospect.' —Andrew Thompson

Read "From the Ground Up" in the Spring 2012 issue of Caltech's Engineering & Science magazine. 

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American Chemical Society Names Caltech Chemist Sarah Reisman a Rising Star

Sarah E. Reisman, an assistant professor of chemistry at Caltech, will receive the WCC Rising Star Award today, making her one of 10 midcareer women chemists to be honored with the award in its inaugural year. The distinction, bestowed by the Women Chemists Committee (WCC) of the American Chemical Society (ACS), will be presented at the society's 243rd national meeting in San Diego and is intended to help promote the retention of women in science.

"We have done a better job in encouraging women into the STEM (science, technology, engineering, and mathematics) fields with higher numbers achieving both Bachelors and Doctoral degrees," said Nancy Jackson, immediate past president of the ACS, in a statement. "However, the actual number of women in mid-career positions continues to decline. I am pleased to see the WCC address this important issue, and the WCC Rising Star Award is a perfect opportunity to highlight successful women chemists to promote retention in the chemical enterprise."

Reisman was cited by the WCC "for excellence in the development of catalytic asymmetric methodologies for natural product synthesis." Her group at Caltech works to develop new ways to synthesize in the laboratory chemical compounds that are produced naturally by plants, bacteria, or fungi.

Reisman explains that her group chooses to work on natural products for two reasons: From a biology standpoint, organisms often make these compounds as mechanisms of chemical warfare—bacteria produce antibiotics to kill other bacteria, for instance. This can make the chemicals desirable for pharmaceutical development. From a chemistry standpoint, she says, "we usually select really complicated, challenging molecules because they require us to develop new chemistry if we want to prepare them in any sort of straightforward fashion."

The Reisman group has recently focused on synthesizing a class of compounds called ETPs, short for the chemical functional group epidithiodiketopiperazine that these compounds contain. ETPs are extremely reactive and participate in a lot of interesting biology, but this reactivity also makes them difficult to work with. Reisman and her colleagues recently published a paper in the Journal of the American Chemical Society describing the synthesis of an ETP called acetylaranotin, which was isolated in the 1960s but had never been prepared synthetically. "It's exciting because it provides the first synthetic access to a particular class of ETP compounds," Reisman says. "We know that they have some promising properties in terms of cancer therapeutics, but they haven't been studied in any detail."

Reisman was born and raised in Bar Harbor, Maine. She earned her BA at Connecticut College in 2001 and her PhD at Yale University in 2006. She was a postdoctoral fellow at Harvard University and joined the faculty at Caltech in 2008.

When she thinks back on her education, she says she fell in love with synthetic organic chemistry when she took her first organic chemistry class as a premed requirement. She quickly realized that she no longer wanted to go to medical school, but instead she wanted to do organic chemistry research.

"What I love about organic chemistry is that it takes the best aspects of scientific research and adds a kind of creative discipline," Reisman says. "When you go in the lab and when you're designing experiments, that's grounded in our scientific method, but before you get into the lab, when you're thinking about how you want to make a given molecule, that's a very creative endeavor, and I really like that aspect. In some ways, it's very much like solving a logic puzzle."

For a complete list of the winners of the inaugural Rising Star Award, click here

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Kimm Fesenmaier
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American Chemical Society Honors Shu-ou Shan

The American Chemical Society (ACS) has honored Shu-ou Shan, professor of chemistry at Caltech, with this year's Nobel Laureate Signature Award for Graduate Education in Chemistry.

According to the ACS website, the purpose of the award is "to recognize an outstanding graduate student and her or his preceptor(s), in the field of chemistry, as broadly defined."

Shan was honored as preceptor along with Xin Zhang, a student at the Scripps Research Institute.

They were selected "for pioneering mechanistic studies on the fidelity of protein targeting mediated by the signal recognition particle system," and they will be honored at an awards ceremony on March 27 in conjunction with the 243rd ACS national meeting in San Diego.

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Allison Benter
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Caltech Study Supports Model for Locating Genetic Damage Through DNA Charge Transport

PASADENA, Calif.—Our genetic information is under constant attack—not only from outside sources such as UV radiation and environmental toxins, but also from oxidative stress, the production of highly reactive forms of oxygen, within our bodies. Luckily, repair proteins are typically hard at work, locating and fixing damaged DNA. Over the past decade, Caltech chemist Jacqueline Barton has been exploring a model that describes how repair proteins might work together in this scouting mission to efficiently home in on lesions or mismatches within the DNA.

Essentially, the model suggests that two DNA-bound repair proteins can use DNA like a wire to shuttle electrons between themselves—a process called charge transport. When one protein receives an electron from the other, its affinity for the DNA to which it clings decreases, causing the protein to fall off that strand. If instead, a lesion—a structural defect in the DNA—prevents that electron from being transferred between the proteins, both members of the pair remain bound to the DNA and begin inching toward the problem area. Since this signaling can be achieved over long molecular distances, the model could explain how it is that the relatively few repair proteins in our cells are able to scour so much genetic information to efficiently locate problems. 

Providing support for that model, Barton's team has recently shown that two different repair proteins that are part of two different genome-maintenance pathways preferentially reposition themselves onto damaged strands of DNA. Publishing in the journal Proceedings of the National Academy of Sciences (PNAS), the group recently reported that repair proteins relocate in this way only if they have the capability to participate in charge transport. In the study, proteins with mutations that destroy their charge-transport capabilities could not zero in on DNA lesions. Versions of those mutated proteins found in humans are associated with diseases such as colorectal cancer, Cockayne syndrome, and xeroderma pigmentosum, suggesting that charge transport may indeed be a necessary part of genome maintenance.

"These findings are consistent with and provide data to support the model of facilitated search for lesions through DNA-mediated signaling between proteins," says Barton, the Arthur and Marian Hanisch Memorial Professor of Chemistry and chair of the Division of Chemistry and Chemical Engineering at Caltech. "This provides another piece of the puzzle."

In their study, the researchers investigated XPD, a protein involved in both DNA repair and replication. First, the scientists attached very short strands of DNA to a gold electrode, added the XPD, and used the electrode to measure the protein's electrical potential, or its ability to send or receive electrons. Separately, the chemists made a solution of the protein along with both regularly matched strands of DNA and longer strands that included a mismatched pair of nucleotides, which are the individual chemical units that make up DNA. Then they used microscopy to visualize and count the number of proteins that bound themselves to the different types of DNA. They found that only the proteins that were able to send and receive electrons through the DNA repositioned themselves in the vicinity of the mismatched nucleotides.

"We believe that the redistribution comes from two proteins using charge transport to communicate with one another, and falling off of the strands that don't have a lesion and attaching to the strands that do," says Pam Sontz, lead author on the study and a graduate student at Caltech.

In a previous study, the Barton lab had conducted similar experiments with Endonuclease III (EndoIII), a repair protein that removes damaged bases. They found that like XPD, EndoIII redistributes itself so that it can home in on mismatches in DNA, and that mutant forms of EndoIII that cannot participate in charge transfer do not relocalize.

In the new study, the researchers were also able to show that mixtures of EndoIII and XPD were able to coordinate in order to relocate onto the mismatched strands of DNA. The team was working with EndoIII from the bacteria Escherichia coli and XPD from a microorganism called Sulfolobus acidocaldarius.

"Our findings suggest that these two proteins are able to signal one another in order to zero in on a lesion," Sontz says. "They're from different DNA-repair pathways and from totally separate organisms, which is really neat. That's what's really opening the door for a lot of future studies. If EndoIII and XPD can do this, there are probably many other proteins from a variety of organisms that are also able to send or receive charge through DNA."

Coauthor and graduate student Tim Mui adds that this kind of cooperation between tested proteins that are normally completely isolated from one another could indicate that the mechanism has been conserved by organisms across evolutionary history. "It's kind of remarkable that these proteins, which should never ever be in contact with one another, can actually coordinate to do this," he says.

The key to this coordination seems to be that the two types of proteins have comparable electrical potentials when bound to DNA, meaning that they are similar in their likelihood to gain or lose electrons. "We're finding that one of the requirements for a protein to potentially participate in this process is that as it binds to DNA, it has to have a similar potential to other proteins, so that it can release an electron that can shuttle through the DNA to another protein," Sontz says. "If the two proteins are not at similar potentials, you're not going to get accurate cooperation."

The proteins have this ability to send and receive electrons because they contain what are called redox-active iron-sulfur clusters. Both XPD and EndoIII contain four-iron, four-sulfur clusters that play no clear structural role in the proteins but contain metals that can easily gain or lose an electron as they bind DNA. "It's really difficult for the cell to build these clusters," Mui says. "So there is a thought that they must play a significant role in something else, which could be this mechanism to locate lesions within the DNA."

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Caltech Professor David Tirrell Named Director of the Beckman Institute

David Tirrell, the Ross McCollum-William H. Corcoran Professor and professor of chemistry and chemical engineering at Caltech, has been appointed director of the Beckman Institute. He succeeds biologist Barbara Wold, who has returned to full-time professorial duties after a decade at the institute's helm.

"We would like to thank Barbara Wold for her dedication to and leadership of the Beckman Institute over the past 10 years," says Stephen Mayo, chair of the Division of Biology. "Under her guidance, the Beckman Institute has truly advanced its mission, enabling the invention of methods, instrumentation, and materials that will provide new opportunities for research at the interface of chemistry and biology."

Tirrell, who is known for work that bridges chemistry, biology, and materials science, served as chair of the division of Chemistry and Chemical Engineering at Caltech from 1999 until 2009. He was chosen for the new position by a search committee chaired by Doug Rees, Caltech's Roscoe Gilkey Dickinson Professor of Chemistry.

"Dave's research interests will serve him well in overseeing the Beckman Institute as will his administrative talents as a former chair of the Division of Chemistry and Chemical Engineering for ten years," says Jacqueline Barton, current chair of the division. "We thank him for this important service to the Institute and look forward to his outstanding leadership."

The Beckman Institute was opened in 1989 in a 160,000-square-foot building on the west end of campus with Harry Gray, the Arnold O. Beckman Professor of Chemistry, as the founding director. Made possible by an initial $50 million commitment and challenge from the Arnold and Mabel Beckman Foundation in 1986, the institute provides space for interdisciplinary work in endeavors such as advanced imaging, laser spectroscopy and X-ray diffraction, synthesis and characterization of novel organic and inorganic materials, and advanced mass spectroscopic methods for characterization of large biomolecules.

Tirrell joined the faculty at Caltech in 1998. He earned his BS from MIT in 1974 and his PhD from the University of Massachusetts in 1978. He became an assistant professor at Carnegie-Mellon University in 1978 and signed on as director of the Materials Research Laboratory at the University of Massachusetts in 1984.

Tirrell is one of only 13 living members of all three branches of the National Academies (Sciences, Engineering, and Medicine). He has also been awarded the Arthur C. Cope Scholar, Carl Marvel, Harrison Howe, S. C. Lind, and Madison Marshall Awards of the American Chemical Society, as well as the ACS Award in Polymer Chemistry.

Tirrell has developed methods for getting bacterial cells to "read" artificial genes and produce protein-like structures with unusual properties. His methods have led to new strategies for the design of therapeutic proteins and to new approaches to the analysis of protein synthesis in cells, tissues, and organisms.

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Kimm Fesenmaier
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Caltech Chemists Devise Chemical Reaction that Holds Promise for New Drug Development

PASADENA, Calif.—A team of researchers at the California Institute of Technology (Caltech) has devised a new method for making complex molecules. The reaction they have come up with should enable chemists to synthesize new varieties of a whole subclass of organic compounds called nitrogen-containing heterocycles, thus opening up new avenues for the development of novel pharmaceuticals and natural products ranging from chemotherapeutic compounds to bioactive plant materials such as morphine.

The team—led by Brian Stoltz, the Ethel Wilson Bowles and Robert Bowles Professor of Chemistry, and Doug Behenna, a scientific researcher—used a suite of specialized robotic tools in the Caltech Center for Catalysis and Chemical Synthesis to find the optimal conditions and an appropriate catalyst to drive this particular type of reaction, known as an alkylation, because it adds an alkyl group (a group of carbon and hydrogen atoms) to the compound. The researchers describe the reaction in a recent advance online publication of a paper in Nature Chemistry.

"We think it's going to be a highly enabling reaction, not only for preparing complex natural products, but also for making pharmaceutical substances that include components that were previously very challenging to make," Stoltz says. "This has suddenly made them quite easy to make, and it should allow medicinal chemists to access levels of complexity they couldn't previously access."

The reaction creates compounds called heterocycles, which involve cyclic groups of carbon and nitrogen atoms. Such nitrogen-containing heterocycles are found in many natural products and pharmaceuticals, as well as in many synthetic polymers. In addition, the reaction manages to form carbon-carbon bonds at sites where some of the carbon atoms are essentially hidden, or blocked, by larger nearby components.

"Making carbon-carbon bonds is hard, but that's what we need to make the complicated structures we're after," Stoltz says. "We're taking that up another notch by making carbon-carbon bonds in really challenging scenarios. We're making carbon centers that have four other carbon groups around them, and that's very hard to do."

The vast majority of pharmaceuticals being made today do not include such congested carbon centers, Stoltz says—not so much because they would not be effective compounds, but because they have been so difficult to make. "But now," he says, "we've made it very easy to make those very hindered centers, even in compounds that contain nitrogen. And that should give pharmaceutical companies new possibilities that they previously couldn't consider."

Perhaps the most important feature of the reaction is that it yields almost 100 percent of just one version of its product. This is significant because many organic compounds exist in two distinct versions, or enantiomers, each having the same chemical formula and bond structure as the other, but with functional groups in opposite positions in space, making them mirror images of each other. One version can be thought of as right-handed, the other as left-handed.

The problem is that there is often a lock-and-key interaction between our bodies and the compounds that act upon them—only one of the two possible hands of a compound can "shake hands" and fit appropriately. In fact, one version will often have a beneficial effect on the body while the other will have a completely different and sometimes detrimental effect. Therefore, it is important to be able to selectively produce the compound with the desired handedness. For this reason, the FDA has increasingly required that the molecules in a particular drug be present in just one form.

"So not only are we making tricky carbon-carbon bonds, we're also making them such that the resulting products have a particular, desired handedness," Stoltz says. "This was the culmination of six years of work. There was essentially no way to make these compounds before, so to all of a sudden be able to do it and with perfect selectivity… that's pretty awesome."

In addition to Stoltz and Behenna, other authors on the paper, "Enantioselective construction of quaternary N-heterocycles by palladium-catalysed decarboxylative allylic alkylation of lactams," include Yiyang Liu, Jimin Kim, David White, and Scott Virgil of Caltech, and Taiga Yurino, who visited the Stoltz lab on a fellowship supported by the Japan Society for the Promotion of Science. The work was supported by the King Abdullah University of Science and Technology, the NIH-NIGMS, the Gordon and Betty Moore Foundation, Amgen, Abbott, and Boehringer Ingelheim. 

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Kimm Fesenmaier
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Caltech Faculty Receive Gates Foundation Grants for Global Health Initiatives

On December 15, the Gates Foundation and Grand Challenge Canada announced over $31 million in new grants to help advance healthcare in the developing world. James Heath, Gilloon Professor and professor of chemistry, and Axel Scherer, Neches Professor of Electrical Engineering, Applied Physics, and Physics, were among the 12 grant recipients who will be funded by the Bill & Melinda Gates Foundation. Caltech was the only organization to receive more than one award.  

The grants are part of the Point-of-Care Diagnostics (POC Dx) Initiative, which aims to create high-quality, low-cost diagnostic platforms to improve the quality and efficacy of healthcare in the world's poorest countries. POC Dx is the 14th program of the Grand Challenges in Global Health initiative, launched in 2003 to create new healthcare tools across a range of disciplines.   

"New and improved diagnostics to use at the point of care can help health workers around the world save countless lives," said Chris Wilson, director of global health discovery at the Bill & Melinda Gates Foundation, in a press release. "Our hope is that these bold ideas lead to affordable, easy-to-use tools that can rapidly diagnose diseases, trigger timelier treatment and thereby reduce death, disability and transmission of infections in resource-poor communities."

Heath was awarded a grant to develop HIV diagnostic tools that use synthetically created peptides instead of antibodies in diagnostic assays. Their chemical structure would allow them to be transported, stored, and used more easily than antibodies. Scherer will work with collaborators at Dartmouth to develop a prototype technology to detect a wide range of pathogens that is low-cost, low-power, and easy to use.

For more information on the Grand Challenges in Global Health program, visit the program's website

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