https://engineering.wustl.edu/news/Pages/Engineers-developing-self-powered-brain-activity-recorders.aspx734Engineers developing self-powered brain activity recorders<p>​Launched in 2013, the Brain Research through Advancing Innovative Neurotechnologies (BRAIN) Initiative is designed to fund research that will ultimately revolutionize the understanding of the human brain, from individual cells to complex neural circuits.<br/></p><img alt="Shantanu Chakrabartty" src="/Profiles/PublishingImages/Chakrabartty_Shantanu.jpg?RenditionID=1" style="BORDER:0px solid;" /><div id="__publishingReusableFragmentIdSection"><a href="/ReusableContent/36_.000">a</a></div><p>The National Institutes of Health recently awarded a two-year, BRAIN Initiative grant to engineers at Washington University in St. Louis. Their goal: to develop a self-sustaining brain implant that can record neural activity patterns over the entire life of an organism.</p><p>"We want to be able to record the neural activity from the brain, but we are going to do it in a very unique way," said <a href="/Profiles/Pages/Shantanu-Chakrabartty.aspx">Shantanu Chakrabartty</a>, professor of electrical & systems engineering at the School of Engineering & Applied Science.</p><p>Instead of directly powering the implant like other neurotechnologies, Chakrabartty plans to use electrical signals generated by the neurons as a power source. The device would continuously record neural activity patterns throughout an organism's lifespan. Since there is no need for external powering or any wireless transmission, the device could be significantly miniaturized to be implanted into the brain of an insect, perhaps someday even a human. </p><blockquote>"It's like plugging a special jump-drive inside the brain," Chakrabartty said.</blockquote>"You continuously log the data and then, when you retrieve the drive, you analyze the data and look for special events that might have occurred during the organism's life-span." These events could then be time correlated with events that are also recorded from other parts of the brain or from the brain of other organisms. <p></p><p>In collaboration with <a href="/Profiles/Pages/Barani-Raman.aspx">Baranidharan Raman</a>, associate professor of biomedical engineering, the research team will first verify the operation of these devices in the brain of the locusts. Using controlled experiments, they will assess how reliably the devices can pick up neural activity specific to olfaction. </p><p>"We know that some traces of the neural activity will be present," Chakabartty said. "The challenge will be: Once we retrieve the device, can we reconstruct what happened? If so, we could ask and answer all sorts of new scientific questions about social interactions, since this tool will be able to measure neural activity when an organism is freely behaving in its natural environment."</p><p> <em>The grant is award R21EY028362 from the National Eye Institute of the National Institutes of Health, as part of the BRAIN Initiative.</em></p> <SPAN ID="__publishingReusableFragment"></SPAN> <p> <em><br/></em></p>Shantanu ChakrabarttyErika Ebsworth-Goold2017-10-12T05:00:00ZThe National Institutes of Health recently awarded a two-year, BRAIN Initiative grant to engineers at Washington University in St. Louis. “We want to be able to record the neural activity from the brain,” said Shantanu Chakrabartty.
https://engineering.wustl.edu/news/Pages/Toolkit-underway-at-WashU-may-give-researchers-insight-into-cancer.aspx731Toolkit underway at WashU may give researchers insight into cancer<p>​By studying the effects of a biochemical process on protein function, Kristen Naegle, a biomedical engineer at Washington University in St. Louis, hopes to identify new therapeutic interventions for cancer.<br/></p><img alt="Kristen Naegle" src="/Profiles/PublishingImages/Naegle_Kristen.jpg?RenditionID=1" style="BORDER:0px solid;" /><div id="__publishingReusableFragmentIdSection"><a href="/ReusableContent/36_.000">a</a></div><p><a href="/Profiles/Pages/Kristen-Naegle.aspx">Kristen Naegle</a>, assistant professor of biomedical engineering in the School of Engineering & Applied Science, has received a three-year, $610,000 grant from the National Institutes of Health’s National Cancer Institute to create a toolkit that will allow biomedical engineers to study the effects of tyrosine phosphorylation, which becomes dysregulated in cancer. The toolkit would be a fast, inexpensive and accessible way for researchers to produce phosphorylated and soluble proteins compared to current methods.</p><p style="color: #000000; font-family: "times new roman"; font-size: medium;"></p><p>Phosphorylation is a process through which a phosphate group is added to a protein by an enzyme called a kinase. It is important in regulating cell signaling but is difficult to study, Naegle said.</p><p style="color: #000000; font-family: "times new roman"; font-size: medium;"></p><p>The funding will allow Naegle’s lab to compare the function of phosphorylated forms of protein domains that are involved in signaling networks with an unphosphorylated form and study their relation to cancer.</p><p style="color: #000000; font-family: "times new roman"; font-size: medium;"></p><p>“We see these phosphorylation sites popping up in cancer and see them regulated by drugs we give to cancer patients,” she says. “It suggests that phosphorylation of these domains is involved in cancer progression. There are enough cancer patient samples to suggest that this is going to be relevant to human health as well as to basic human development.”</p><p style="color: #000000; font-family: "times new roman"; font-size: medium;"></p><p>Naegle has a patent pending on the technology and is working with the university’s Office of Technology Management.</p><p style="text-align: center;"><img src="/news/PublishingImages/Kristen%20Naegle%20Proteins%20WashU%20Engineering%20amino%20acid%20substitution.png" class="ms-rtePosition-4" alt="" style="margin: 5px;"/><br/></p><p><br/></p><SPAN ID="__publishingReusableFragment"></SPAN><br/>Kristen NaegleBeth Miller2017-10-10T05:00:00ZBy studying the effects of a biochemical process on protein function, Assistant Professor Kristen Naegle hopes to identify new therapeutic interventions for cancer.
https://engineering.wustl.edu/news/Pages/Imaging-a-killer.aspx729Imaging a killer<div class="youtube-wrap"><div class="iframe-container"> <iframe width="854" height="480" frameborder="0" src="https://www.youtube.com/embed/_5ldqyK0S2Y"></iframe>   <br/><br/></div></div><img alt="" src="/news/PublishingImages/WashU%20Engineering%20Huntingtons.jpg?RenditionID=1" style="BORDER:0px solid;" /><div id="__publishingReusableFragmentIdSection"><a href="/ReusableContent/36_.000">a</a></div><p>​​Huntington’s disease is a progressive, fatal neurodegenerative disorder that is caused by mutations in one specific gene called huntingtin (Htt). In the 20-plus years since the Htt gene was identified, researchers have focused on the protein encoded by the Htt gene, called Httex1. This protein accumulates in the brains of Huntington’s disease patients, and the prevailing hypothesis has been that it undergoes a dramatic structural change when a repetitive tract of the amino acid glutamine mutates into an aberrantly long region known as the mutationally expanded polyglutamine (polyQ) tract.</p><p>Now, for the first time, the team of <a href="http://lashuel-lab.epfl.ch/">Hilal A. Lashuel at Ècole Polytechnique Fèdèrale de Lausanne</a> (EPFL) in Switzerland; Edward A. Lemke at the European Molecular Biology Laboratory (EMBL) in Germany; and <a href="/Profiles/Pages/Rohit-Pappu.aspx">Rohit V. Pappu</a> at Washington University in St. Louis has uncovered a detailed structural description of Htt as a function of polyQ length. The work was published recently in the <a href="http://pubs.acs.org/doi/pdf/10.1021/jacs.7b06659">Journal of the American Chemical Society.</a><br/></p><h3>A study in three steps</h3><p>Securing atomic-level structural descriptions of full-length Htt and disease-relevant protein fragments referred to as Httex1 have been challenging because these molecules stick to one another and inhibit the generation of pure protein samples for structural studies. “It is very difficult to obtain structural characterization of proteins within a mush,” said Pappu, the Edwin H. Murty Professsor of Engineering in the School of Engineering & Applied Science.<br/></p><p>“Our goal was to gain insight into how increasing the length of the polyQ tail repeat alters structure of this protein at the monomer level and under conditions where we are able to unlink its folding and self-assembly,” said Lashuel, professor of life sciences and director of the laboratory of the chemical biology of neurodegeneration at EPFL.</p><p>In the first step of the study, Lashuel and postdoctoral fellow John B. Warner IV used novel chemical strategies in their lab to produce precise, high-purity samples of Htt for molecular spectroscopy. But these only came in ultra-low concentrations and required techniques that probe individual molecules. Warner and Lashuel enabled these experiments by generating samples with site-specific fluorescent labels.</p><p>For the second step of the project, Warner and Lashuel worked with Lemke’s lab at EMBL to perform single-molecule Förster (or fluorescence) resonance energy transfer (smFRET), which is a technique that can measure distances between 1-10 nanometers within individual molecules — in this case, within individual Htt proteins. This part of the study yielded the first quantitative assessment of how the inter-atomic distances within Httex1 vary with the expansion mutations.</p><p>Finally, the scientists worked with Pappu’s lab at Washington University, where it developed novel computer modeling approaches to produce physically accurate, atomic-level structural models of Httex1 that best fit all of the single-molecule data from the previous two steps. The results were surprising: The overall structure of Httex1 resembles that of a tadpole.<br/></p><h3>The tadpole effect<br/></h3><p>“Architecturally, Httex1 is tadpole-shaped, with a globular polyQ head and a floppy tail,” Pappu said. “As the polyQ length gets longer, the head of the tadpole becomes larger in its surface area. This increased surface area of the head appears to engender interactions that otherwise shouldn’t be present in cells.”</p><p>The discovery challenges the longstanding ideas about Httex1 accumulation in Huntington’s disease. “If the prevailing hypothesis were true,” Pappu said, “then the tadpole would have turned into a ‘frog’ as the polyQ length increases above the threshold length, but that does not appear to be the case. The new results instead focus our attention on the novel gain-of-function cellular interactions that are driven by the tadpole structure with a larger polyQ head.”</p><p>“While the prevailing hypothesis has favored a model where mutant huntingtin-induced toxicity is driven mainly by its propensity to misfold and aggregate, our findings suggest that aberrant interactions at the monomer level may also contribute to the initiation and/or progression of the disease,” Lashuel said.</p><p>“This finding allows us to examine what regions of this protein are important to target, and modulate its toxicity in a specific manner,” said Kiersten M. Ruff, a postdoctoral fellow in Pappu’s lab who designed the computer simulations and is the co-first author on the paper.</p><p>The next challenge for the scientists is to understand how these structural changes at the monomer level of Httex1 translate into increased aggregation and toxicity when the length of the polyQ tail crosses the pathogenic threshold.</p><p>“The key has been the centrality of collaboration among three teams with complementary and non-overlapping expertise, all sharing a commitment to advancing science,” Lashuel said.</p><hr style="height: 1px; background-color: #c8c8c8; border-top-width: 0px; margin-bottom: 1.5em; color: #3c3d3d; font-family: "source sans pro", "helvetica neue", helvetica, arial, sans-serif; font-size: 19.2px;"/><p>Funding for this research was provided by the CHDI Foundation, EPFL, the National Institutes of Health and EMBL (EIPOD, under Marie Curie Actions COFUND).</p><p>John B Warner IV*, Kiersten M. Ruff*, Piau Siong Tan, Edward A. Lemke, Rohit V. Pappu§, Hilal A. Lashuel§. (*Co-first authors; §Co-corresponding authors) Monomeric huntingtin exon 1 has similar overall structural features for wild type and pathological polyglutamine lengths. “Journal of the American Chemical Society” 22 September 2017. DOI: 10.1021/jacs.7b06659<br/></p><SPAN ID="__publishingReusableFragment"></SPAN><p><br/></p>​ <div><div class="cstm-section"><h3>Rohit Pappu<br/></h3><div style="text-align: center;"> <strong> <a href="/Profiles/Pages/Rohit-Pappu.aspx"> <img src="/Profiles/PublishingImages/Pappu_Rohit_1_16_05.jpg?RenditionID=3" alt="Yixin Chen" style="margin: 5px;"/></a> <br/> </strong> </div><div style="text-align: center;"> <span style="font-size: 12px;">Professor<br/>Biomedical Engineering<br/><a href="/Profiles/Pages/Rohit-Pappu.aspx">>> View Bio</a></span></div><div></div></div> <br/> </div> <br/>An international cohort of scientists, including engineers from Washington University in St. Louis, recently visualized Huntington's protein for the first time.2017-10-09T05:00:00ZAn international team of researchers has obtained the first ever atom-level structural insights into Httex1, a part of the gene that is thought to cause the devastating neurological disorder Huntington’s disease.<p>International team finds high-resolution structural analysis of protein behind Huntington’s<br/></p>
https://engineering.wustl.edu/news/Pages/Spartan-Makerspace-will-foster-innovation-and-entrepreneurship.aspx726Spartan Makerspace will foster innovation and entrepreneurship<p>​“I believe making things with your hands is essential to being a truly well-rounded engineer,” says Washington University Trustee Donald Jubel, BS ’73, chief executive officer of Spartan Light Metal Products. “You can learn the nuances of using different materials. You also learn to have respect for the people who actually make products. I have designed things that have turned out to be almost impossible to make. Learning from your mistakes is a great teacher.”<br/></p><img alt="" src="/news/PublishingImages/Spartan-Light-Metal-Products-Maker-SpaceFINAL-1aj0guj.jpg?RenditionID=1" style="BORDER:0px solid;" /><p>​To give Washington University students enhanced opportunities to learn by working with their hands, Spartan has pledged $1 million to create the Spartan Light Metal Products Maker Space. The cutting-edge facility will be centrally located on the ground floor of <a href="https://campusnext.wustl.edu/items/henry-a-and-elvira-h-jubel-hall/">Henry A. and Elvira H. Jubel Hall</a>, which was named in 2013 with a substantial commitment from the Jubel family through the Henry A. Jubel Foundation. Jubel Hall, part of the university’s east end transformation project, will be completed in 2019 and will house the Department of Mechanical Engineering & Materials Science in the School of Engineering & Applied Science.<br/></p><p>The Spartan Makerspace will transform the way students and faculty members interact with their subject matter in many areas of study. Its state-of-the-art resources will include 3D printers and scanners, plasma cutters, computer-controlled milling machines, and lathes for cutting metal. Such tools can be used to create everything from tech products and biomedical devices to sculptures and architectural mock-ups.</p><blockquote>“The makerspace will accelerate innovation and entrepreneurship across Washington University,” says<a href="/Profiles/Pages/Philip-Bayly.aspx"> Philip Bayly</a>, chair of mechanical engineering and the Lilyan and E. Lisle Hughes Professor. “It will provide a place where innovators can bring to life designs for addressing society’s challenges.</blockquote> <p>“For entrepreneurs, working prototypes are a huge help in demonstrating an idea in order to obtain patent protection, convince investors, and attract customers,” he adds. “The Spartan Makerspace will provide students and faculty with sophisticated fabrication capabilities that will allow them to have an even greater impact on our world.”</p><p>In 1961, Donald Jubel’s father, Henry Jubel, BS ’40, founded Spartan Light Metal Products, which has become an industry leader in the design and manufacture of aluminum and magnesium custom diecasting products and assemblies. He attributed his success to his Washington University education. Beginning with Henry, three generations of the Jubel family have earned degrees in mechanical engineering at the university, including Donald and his daughter Lindsey, BS ’09, MS ’09.</p><p>For decades, the Jubel family has provided extraordinary support and leadership for Washington University. The family and its foundation have directed significant gifts and annual support to scholarships and programs in the engineering school and to the Alvin J. Siteman Cancer Center. Among his many roles, Donald is a member of the engineering school’s national council and the university’s Alumni Board of Governors. His daughter Melissa Markwort, EMBA ’14, is a member of the LEAD Initiative committee for the engineering school and the Family Business Steering Committee for Olin Business School. She also serves as chair of the Fellows Committee for the William Greenleaf Eliot Society.</p><p>“The Jubels have championed both education and manufacturing in our region and beyond,” Professor Bayly says. “It means a great deal to the university for the maker space to bear the Spartan name.”<br/></p><br/><br/><br/> <span> <div class="cstm-section"><h3>Henry A. and Elvira H. Jubel Hall Details<br/></h3><div> <strong></strong></div><div><ul style="padding: 0px; margin: 0px 0px 1.33333em 1em; z-index: 0; color: #555555; font-family: "source sans pro", "helvetica neue", helvetica, arial, sans-serif; font-size: 18px;"><li style="line-height: 1.33333; left: 1em; margin-top: 0.44444em; margin-bottom: 0.44444em; margin-right: 1em;"><p>80,600 square ft. <br/></p></li><li><p>15,600 sq. ft. research lab space</p></li><li><p>7,850 sq. ft. faculty offices</p></li><li><p>3,350 sq. ft. makerspace <br/></p></li><li><p>Located south of Whitaker Hall, east of the Hub, and north of the new Ann and Andrew Tisch Park<br/></p></li><li style="line-height: 1.33333; left: 1em; margin-top: 0.44444em; margin-bottom: 0.44444em; margin-right: 1em;"><p>Two 65-seat pooled classrooms<br/></p></li><li style="line-height: 1.33333; left: 1em; margin-top: 0.44444em; margin-bottom: 0.44444em; margin-right: 1em;"><p><a href="https://campusnext.wustl.edu/items/henry-a-and-elvira-h-jubel-hall/">More details</a><br/></p></li></ul></div></div></span>“It (Spartan Light Metal Products Makerspace) is designed to pique interest,” Donald Jubel says. “Who knows, it may lead some students to change their major to engineering!”Kelly Marksburyhttp://together.wustl.edu/Pages/Jubel-Maker-Space.aspx2017-10-03T05:00:00ZThe new makerspace will include 3-D printers and scanners, plasma cutters, computer-controlled milling machines, and lathes for cutting metal.
https://engineering.wustl.edu/news/Pages/Chemo-loaded-nanoparticles-target-breast-cancer-that-has-spread-to-bone.aspx724Chemo-loaded nanoparticles target breast cancer that has spread to bone<p>​Breast cancer that spreads often infiltrates bone, causing fractures and intense pain. In such cases, chemotherapy is ineffective because the environment of the bone protects the tumor, even as the drug has toxic side effects elsewhere in the body.<br/></p><img alt="" src="/news/PublishingImages/NanoBoneMetastaticBC-760.jpg?RenditionID=1" style="BORDER:0px solid;" /><p>Now, scientists at Washington University School of Medicine in St. Louis have developed a nanoparticle that can deliver chemotherapy directly to tumor cells that have spread to bone. In mice implanted with human breast cancer and exposed to circulating cancer cells likely to take up residence in bone, the researchers showed the treatment kills tumor cells and reduces bone destruction while sparing healthy cells from side effects.</p><p>The study is available online in the journal Cancer Research.</p><p>“For women with breast cancer that has spread, 70 percent of those patients develop metastasis to the bone,” said senior author <a href="https://wuphysicians.wustl.edu/for-patients/find-a-physician/katherine-nelson-weilbaecher" target="_blank" rel="noopener">Katherine N. Weilbaecher, MD</a>, a professor of medicine. “Bone metastases destroy the bone, causing fractures and pain. If the tumors reach the spine, it can cause paralysis. There is no cure once breast cancer reaches the bone, so there is a tremendous need to develop new therapies for these patients.”</p><p>In the study, the researchers showed that breast cancer cells that spread to bone carry molecules on their surface that are a bit like Velcro, helping tumor cells stick to the bone. These adhesion molecules also sit on the surface of cells responsible for bone remodeling, called osteoclasts.</p><blockquote>“In healthy bones, osteoclasts chew away old, worn out bone, and osteoblasts come in and build new bone,” said Weilbaecher, who treats patients at <a href="https://siteman.wustl.edu/" target="_blank" rel="noopener">Siteman Cancer Center</a> at Barnes-Jewish Hospital and Washington University School of Medicine. “But in cancer that spreads to bone, tumors take over osteoclasts and essentially dig holes in the bone to make more room for the tumor to grow.”</blockquote> <p>Weilbaecher said she and her colleagues were surprised to find that the same adhesive molecule on the surface of osteoclasts also is present in high levels on the surface of the breast tumors that spread to bone. The research showed that the molecule — called integrin αvβ3 — was absent from the surfaces of the original breast tumor and from tumors that spread to other organs, including the liver and the lung. The researchers confirmed that this pattern also was true in biopsies of human breast tumors that had spread to different organs.</p><p>A collaboration with co-senior author <a href="https://cardiology.wustl.edu/faculty/gregory-m-lanza-md-phd-facc/" target="_blank" rel="noopener">Gregory M. Lanza, MD, PhD</a>, a professor of medicine and of biomedical engineering, then led to the design of a nanoparticle that combines the bone-adhesion molecules with a form of the cancer drug docetaxel, which is used to treat breast cancer as well as other tumors. The adhesive molecules allow the nanoparticle to penetrate the otherwise protective environment of the bone matrix in a way that, in essence, mimics the spreading of the tumor cells themselves. The result is a delivery method that keeps the chemotherapy drug contained in the nanoparticle until the adhesion molecules make contact with the tumor cell, fusing the nanoparticle with the cell surface and releasing the drug directly into the cancer cell.</p><p>“When we gave these nanoparticles to mice that had metastases, the treatment dramatically reduced the bone tumors,” Weilbaecher said. “There was less bone destruction, fewer fractures, less tumor. The straight chemo didn’t work very well, even at much higher doses, and it caused problems with liver function and other toxic side effects, which is our experience with patients. But if we can deliver the chemo directly into the tumor cells with these nanoparticles that are using the same adhesive molecules that the cancer cell uses, then we are killing the tumor and sparing healthy cells.”<br/></p> <span><hr/></span> <div>This work was supported the National Institutes of Health (NIH), grant numbers CA154737, CA100730, CA097250, HL122471, HL112518, HL113392, HHSN26820140042C, P30CA091842, CA143057, CA69158, 5T32GM007067-39, T32AR060719, 5T32CA113275-07 and GM07200; the St. Louis Men’s Group Against Cancer; Siteman Cancer Center; the Washington University Center for Cellular Imaging, supported by Washington University School of Medicine, the Children’s Discovery Institute of Washington University and St. Louis Children’s Hospital, grant number CDI-CORE-2015-505; the National Institute for Neurological Disorders and Stroke, grant number NS086741; The Foundation for Barnes-Jewish Hospital. Technical support was provided by the Washington University Musculoskeletal Research Center, grant number P30AR057235; the Hope Center Alafi Neuroimaging Lab, shared instrumentation grant S10 RR027552; the Molecular Imaging Center at Washington University, grant number P50 CA094056; and the St. Louis Breast Tissue Registry funded by the Department of Surgery at Washington University School of Medicine in St. Louis.<br/><br/>Ross MH, Esser AK, Fox GC, Schmieder AH, Yang X, Cui G, Pan D, Su X, Xu Y, Novack DV, Walsh T, Colditz GA, Lukaszewicz GH, Cordell E, Novack J, Fitzpatrick JAJ, Waning DL, Mohammad KS, Guise TA, Lanza GM, Weilbaecher KN. Bone-induced expression of integrin β3 on breast cancer metastases enables targeted nanotherapy. Cancer Research. Aug. 30, 2017.<br/><br/><a href="http://medicine.wustl.edu/">Washington University School of Medicine</a>’s 2,100 employed and volunteer faculty physicians also are the medical staff of <a href="http://www.barnesjewish.org/">Barnes-Jewish</a> and <a href="http://www.stlouischildrens.org/">St. Louis Children’s</a> hospitals. The School of Medicine is one of the leading medical research, teaching and patient-care institutions in the nation, currently ranked seventh in the nation by U.S. News & World Report. Through its affiliations with Barnes-Jewish and St. Louis Children’s hospitals, the School of Medicine is linked to <a href="http://www.bjc.org/">BJC HealthCare</a>.<br/><br/><a href="https://siteman.wustl.edu/">Siteman Cancer Center</a>, ranked among the top cancer treatment centers by U.S. News & World Report, also is one of only a few cancer centers to receive the highest rating of the National Cancer Institute (NCI) – “exceptional.” Comprising the cancer research, prevention and treatment programs of <a href="http://www.barnesjewish.org/">Barnes-Jewish Hospital</a> and <a href="http://medicine.wustl.edu/">Washington University School of Medicine</a> in St. Louis, Siteman treats adults at five locations and partners with <a href="http://www.stlouischildrens.org/">St. Louis Children’s Hospital</a> in the treatment of pediatric patients. Siteman is Missouri’s only NCI-designated Comprehensive Cancer Center and the state’s only member of the National Comprehensive Cancer Network. Through the <a href="https://siteman.wustl.edu/visiting/network/">Siteman Cancer Network</a>, Siteman Cancer Center works with regional medical centers to improve the health and well-being of people and communities by expanding access to cancer prevention and control strategies, clinical studies and genomic and genetic testing, all aimed at reducing the burden of cancer.<br/></div>Seeking new treatments for metastatic breast cancer, researchers have designed nanoparticles (shown in magenta) that carry chemotherapy and are targeted directly to tumors that have spread to bone. Julia Evangelou Strait https://source.wustl.edu/2017/09/chemo-loaded-nanoparticles-target-breast-cancer-spread-bone/2017-09-25T05:00:00ZResearch in mice showed the treatment kills tumor cells and reduces bone destruction while sparing healthy cells from side effects.<p>Treatment makes chemo more effective, less toxic, mouse study shows<br/></p>