Category Archives: Biochemistry

Biochemistry

Toxic Protein, Linked to Alzheimer’s and Other Neurodegenerative Diseases, Exposed in New Detail – P&T Community

NEW YORK, Feb. 6, 2020 /PRNewswire/ -- The protein tau has long been implicated in Alzheimer's and a host of other debilitating brain diseases. But scientists have struggled to understand exactly how tau converts from its normal, functional form into a misfolded, harmful one. Now, researchers at Columbia University's Zuckerman Institute and Mayo Clinic in Florida have used cutting-edge technologies to see tau in unprecedented detail. By analyzing brain tissue from patients, this research team has revealed that modifications to the tau protein may influence the different ways it can misfold in a person's brain cells. These differences are closely linked to the type of neurodegenerative disease that will develop and how quickly that disease will spread throughout the brain.

The study, published today in Cell, employed two complementary techniques to map the structure of tau and decipher the effects of additional molecules, called post-translational modifications (PTMs), on its surface. These new structural insights could accelerate the fight against neurodegenerative diseases, by helping researchers identify new biomarkers that detect these disorders before symptoms arise and design new drugs that target specific PTMs, preventing the onset of disease before it wreaks havoc on the brain.

"Tau has long been a protein of significant interest due to its prevalence in disease," said Anthony Fitzpatrick, PhD, a Principal Investigator at Columbia's Mortimer B. Zuckerman Mind Brain Behavior Institute who led the study. "In today's publication, we lay out compelling evidence that PTMs play an important structural role in tauopathies, the collection of neurodegenerative diseases characterized by toxic buildup of misfolded tau."

No two tauopathies are exactly alike. Each affects different parts of the brain even different cell types which can lead to different symptoms. Alzheimer's, for example, arises in the hippocampus, and so affects memory. Chronic traumatic encephalopathy, a disorder most often seen in survivors of traumatic brain injury, can lead to problems with movement, memory or emotion, depending on which areas of the brain are affected.

Scientists have used traditional imaging techniques to find clues to how tangles of tau, comprised of individual fibers, or filaments, are implicated in these diseases. But painting a complete picture has proven difficult.

"The brains of patients with neurodegenerative diseases are easy to identify: entire sections have been eaten away, replaced by large clumps and tangles of misfolded proteins like tau," said Tamta Arakhamia, an undergraduate at Columbia's School of General Studies, a research assistant in the Fitzpatrick lab and the paper's co-first author. "However, tau filaments are 10,000 times thinner than the width of a human hair, making them extraordinarily difficult to study in detail."

To address this challenge, Dr. Fitzpatrick recently pioneered the use of cryo-electron microscopy, or cryo-EM, to visualize individual tau filaments from diseased human brain tissue. Cryo-EM is a Nobel Prize-winning technology developed, in part, by researchers at Columbia University. Cryo-EM images samples using a beam of electrons and has proven indispensable for investigations into extremely small biological structures. Using cryo-EM, Dr. Fitzpatrick's team has reconstructed the structures of tau filaments, providing new insights into how they form, grow, and spread throughout the brain.

For all its ability to provide highly detailed snapshots of proteins, cryo-EM has limits. To overcome these limits, Dr. Fitzpatrick and his team to paired it with a second technology: mass spectrometry.

"Cryo-EM does not provide a complete picture because it cannot fully recognize the microscopic PTMs on tau's surface," said Christina Lee, an undergraduate student at Columbia College, a research assistant in the Fitzpatrick lab and the paper's co-first author. "But mass spectrometry can pinpoint the chemical composition of PTMs on the surface of tau."

Working with co-corresponding author Leonard Petrucelli, PhD, Ralph B. and Ruth K. Abrams Professor of Neuroscience at Mayo Clinic in Florida, and Nicholas Seyfried, PhD, professor of biochemistry at Emory University School of Medicine, the researchers used cryo-EM and mass spectrometry to analyze the brain tissue from patients diagnosed with two tauopathies: Alzheimer's disease and corticobasal degeneration, or CBD. CBD is a rare but extremely aggressive tauopathy, affecting only one in every 10,000 people. Unlike Alzheimer's, which is thought to arise due to a number of factors including tau, CBD is primarily associated with misbehaving tau proteins.

"Studying a primary tauopathy like CBD helps us to figure out how tau becomes toxic to brain cells," said Dr. Petrucelli. "We hope to extrapolate that knowledge to secondary tauopathies, such as Alzheimer's disease."

The scientists' analysis of brain tissue samples revealed several key insights. Most notably, the researchers found that cross-talk between PTMs on the surface of tau influences the structure of the tau filaments, contributing to differences in tau filaments observed across the various tauopathies and even variations from patient to patient.

"Collectively, these results suggest that PTMs may not only be serving as markers on the proteins' surface, but are actually influencing the behavior of tau," said Dr. Fitzpatrick, who is also an assistant professor of biochemistry and molecular biophysics at Columbia's Vagelos College of Physicians and Surgeons.

Moving forward, Dr. Fitzpatrick and his team plan to expand this work to other tauopathies. Today's findings on Alzheimer's and CBD hold immense promise for the field, particularly in the development of new disease models such as lab-grown organoids, or mini-brains that may serve to accurately recapitulate what is actually happening in the brains of patients.

"Our findings will inspire new approaches for developing diagnostic tools and designing drugs, such as targeting PTM vulnerabilities to slow disease progression," said Dr. Fitzpatrick, who is also a member of Columbia's Taub Institute for Research on Alzheimer's Disease and the Aging Brain. "Neurodegenerative diseases are among the most complex and distressing class of illnesses, but through our work and that of our colleagues and collaborators, we are building a roadmap toward successful diagnostics and therapeutics."

This paper is titled "Posttranslational modifications mediate the structural diversity of tauopathy strains." Additional contributors include Yari Carlomagno, PhD, Duc Duong, Sean Kundinger, Kevin Wang, Dewight Williams, PhD, Michael DeTure, PhD, Dennis Dickson, MD, and Casey Cook, PhD.

This research was supported by the National Institutes of Health/National Institute of Neurological Disorders and Stroke and National Institute on Aging (U01NS110438, RF1AG056151, R35NS097273, U01NS110438-02, P01NS084974, P01NS099114, R01NS088689, RF1AG062077-01, RF1 AG062171-01, U54NS100693, R01AG053960, R01AG061800, U01AG046161, U01AG061357, S10RR23057, S10OD018111, U24GM116792), NYSTAR and the NIH (GM103310), the National Science Foundation (MRI Grant 1531991, DBI-1338135, DMR-1548924), the Simons Foundation (349247), the Mayo Clinic Foundation, the Association for Frontotemporal Degeneration, the Dana Foundation and the Cure Alzheimer's Fund.

The authors report no financial or other conflicts of interest.

Columbia University'sMortimer B. Zuckerman Mind Brain Behavior Institutebrings together a group of world-class scientists and scholars to pursue the most urgent and exciting challenge of our time: understanding the brain and mind. A deeper understanding of the brain promises to transform human health and society. From effective treatments for disorders like Alzheimer's, Parkinson's, depression and autism to advances in fields as fundamental as computer science, economics, law, the arts and social policy, the potential for humanity is staggering. To learn more, visit:zuckermaninstitute.columbia.edu.

Contact:Anne Holden, anne.holden@columbia.edu,212.853.0171

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Toxic Protein, Linked to Alzheimer's and Other Neurodegenerative Diseases, Exposed in New Detail - P&T Community

Biochemistry

Dyne Therapeutics Expands Leadership Team with Key Hires – Business Wire

WALTHAM, Mass.--(BUSINESS WIRE)--Dyne Therapeutics, a biotechnology company pioneering targeted therapies for patients with serious muscle diseases, today announced the addition of three key members to its leadership team: Oxana Beskrovnaya, Ph.D., senior vice president and head of research; Chris Mix, M.D., senior vice president, clinical development; and John Najim, vice president, chemistry, manufacturing and controls (CMC).

Dyne is establishing a leadership position in muscle disease therapeutics by combining transformative science with an organizational passion for changing the lives of patients, said Joshua Brumm, president and chief executive officer of Dyne. We are thrilled to welcome Oxana, Chris and John to our growing team. Leveraging their collective experience in the discovery and development of novel medicines, we are poised to rapidly advance our programs toward the clinic and are fully focused on execution.

Dr. Beskrovnaya is an accomplished R&D leader with a strong track record of discovering and developing first-in-class therapeutics for rare genetic diseases. Prior to joining Dyne, she served as head of musculoskeletal and renal research in Sanofis rare disease and neurological unit, where she advanced a pipeline of drug candidates using multiple therapeutic modalities, including nucleic acids, proteins and small molecules. Dr. Beskrovnaya is the author of numerous patents, invited reviews, editorials, book chapters and original research articles in major scientific journals. She received her Ph.D. in genetics from Moscow Genetics Institute, followed by postdoctoral fellowship training in neuromuscular diseases at the Howard Hughes Medical Institute at the University of Iowa.

Dr. Mix brings extensive clinical development experience to Dyne, most recently serving as vice president of rare genetic disease clinical development at Agios Pharmaceuticals, where he oversaw development across several hemolytic anemia indications. In his previous role as vice president of clinical development at Sarepta Therapeutics, he focused on advancing candidate therapies for rare neuromuscular disease. Dr. Mix received his B.A. in chemistry from Haverford College and his M.D. from the University of Massachusetts Medical School. He completed his residency in internal medicine at Tufts Medical Center, a fellowship in nephrology at the Beth Israel Deaconess Medical Center in Boston and an M.S. in clinical care research at the Tufts School of Biomedical Sciences.

Mr. Najim brings a wealth of CMC biopharmaceutical development and cGMP manufacturing experience across multiple biologic expression systems and small molecules. Mr. Najim previously held roles of increasing responsibility at Proteon Therapeutics, including most recently as vice president of manufacturing and process development, and also served as associate director of manufacturing at Dyax Corporation. He received his B.S. in biochemistry from Merrimack College and his MBA from Bentley University.

About Dyne TherapeuticsDyne Therapeutics is pioneering life-transforming therapies for patients with serious muscle diseases. The companys FORCE platform delivers oligonucleotides and other molecules to skeletal, cardiac and smooth muscle with unprecedented precision to restore muscle health. Dyne is advancing treatments for myotonic dystrophy type 1 (DM1), Duchenne muscular dystrophy (DMD) and facioscapulohumeral muscular dystrophy (FSHD). Dyne was founded by Atlas Venture and is headquartered in Waltham, Mass. For more information, please visit http://www.dyne-tx.com, and follow us on Twitter and LinkedIn.

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Dyne Therapeutics Expands Leadership Team with Key Hires - Business Wire

Biochemistry

The Different Types of Immunostaining – News-Medical.net

Immunostaining encompasses numerous techniques that are suited to a variety of different applications.

Image Credit: Jarun Ontakrai/Shutterstock.com

However, they are all methods that rely on the use of antibodies to detect and identify proteins within biological samples. They can be used to asses and identify the topographical distribution of abnormal cells, blasts infiltrates, and megakaryocytes.

The term was coined back in 1941 when it was first used to describe immunohistochemical staining. These days, immunohistochemical staining is just one of several established immunostaining techniques, including enzyme-linked immunosorbent assay, flow cytometry, immuno-electron microscopy, and Western blotting.

The techniques are commonplace in biology and molecular biology labs, and are used for a variety of applications in a wide range of fields of study, from oncology to hydrobiology.

Here, we describe the five types of immunostaining techniques.

The enzyme-linked immunosorbent assay, also known as ELISA, is commonly used in biochemistry. Developed in 1971 by Engvall and Perlmann, the method quantifies peptides, proteins, antibodies, and hormones present in a sample by immobilizing an antigen on a solid surface before it is complexed with an antibody that is associated with an enzyme.

Identification is then possible when the conjugated enzyme activity is assessed through incubation with a substrate, resulting in a measurable product.

When the physical and chemical characteristics of cells or particles are sought to be determined, flow cytometry is often the most suitable method. The technique was established in the 1950s, and over the decade's many advancements have been achieved in its methodology and equipment. Currently, measurements are made from cells in solution while they travel through the instruments laser at speeds of 10,000 cells per second. Flow cytometry offers benefits to the technicians who choose to use it, including high sample throughput speed, making it an attractive option as an immunostaining assay.

Immuno-electron microscopy, also referred to as EM immunolabelling and immuno-EM, is a technique that tags antibody molecules with electron-dense substances, usually, and most effectively, being small gold particles, which are seen during the analysis as easy to spot dark dots. The assay allows for the simultaneous detection of more than one type of molecule because particles of different sizes can be used to tag different antibodies.

The technique was first developed as a diagnostic aid that assisted in the detection and identification of viruses, such as gastroenteritis and rotavirus. Today it is still used to diagnosis a variety of viral infections. It is considered to be one of the most sensitive and rapid methods for this application.

The most common application of immunostaining is immunohistochemistry, which is used to assist in the diagnosis of various diseases, including different types of cancer. It has also shown its use in neuropathology, and hematopathology, helping in the classification of diseases in these groups and evolving criteria for their diagnosis. Another area in which it has made a significant impact is that of genetic study, where it has been used to determine the role of specific gene products, elucidating their function in vital biological processes. The technique has become invaluable to both medical research and clinical diagnostics.

The method involves selectively identifying antigens in a sample of cells within a tissue section through the principle that certain antibodies will bind to specific antigens present in the tissue. It was established back in the 1930s before it was first reported in 1941.

The initial principle outlined that antibodies labeled with a fluorescent dye could detect pneumococcal antigens in infected tissues. Since then, the technique has been developed, and new enzyme labels have been introduced, including peroxidase, alkaline phosphatase, and colloidal gold. The use of radioactive elements has also been developed for use with autoradiography.

The final immunostaining method is the Western blot method, a widely used technique that has firmly ingrained itself in the fields of cell and molecular biology. Western blot allows researchers to determine and quantify the proteins existent within a cell, identifying specific proteins out of the mixture of proteins that are present in cell samples.

There are three parts to the Western blot method, the first is separation by size, the second being transfer to a solid support, and finally, a target protein is marked using a suitable primary and secondary antibody to visualize it.

Immunostaining methods have become essential to numerous branches of scientific study, they have also become well established in various clinical applications, mostly in assisting in diagnosis as well as determining characteristics that facilitate more accurate diagnostic criteria.

Since the immunohistochemistry technique was first reported on in 1941, four further types of immunostaining techniques have emerged: enzyme-linked immunosorbent assay, flow cytometry, immuno-electron microscopy, and Western blotting. These methods are being expanded and developed on all the time, growing their use in different applications, and improving on their accuracy and reliability.

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The Different Types of Immunostaining - News-Medical.net

Biochemistry

Biology / Biochemistry News from Medical News Today

2004-2020 Healthline Media UK Ltd, Brighton, UK, a Red Ventures Company. All rights reserved. MNT is the registered trade mark of Healthline Media. Any medical information published on this website is not intended as a substitute for informed medical advice and you should not take any action before consulting with a healthcare professional.

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Biochemistry

Department of Biochemistry School of Medicine

The graduate program in Biochemistry began in 1960 starting with the offering of Masters in Science (M.S.) and doctor in Philosophy (Ph.D.) degrees in Biochemistry and Nutrition. The name of the department was changed in 1992 to Department of Biochemistry. The graduates of our program can be found throughout the industrial, academic and government environment in Puerto Rico, the U.S. mainland and in Latin America. The department faculty actively seeks external funds to support our graduate students and have been able to improve our research facilities with state of the art instrumentation.

The Department of Biochemistry characterizes itself by conducting research in the following areas: Molecular and Genetic Alterations in Disease, Biochemistry of Proteins, Protein Structure/Function Relationships, Biochemistry of Glycoconjugates and Cellular Differentiation, Interactions between Nutrition and Disease, Aging and Oxidative Stress, Ocular Biochemistry, Clinical Biochemistry, Analytical Biochemistry, Biochemical and Molecular Toxicology, Biochemical Pharmacology and Molecular Biology. Individual faculty members also participate as mentors in the Intercampus Ph.D. program in Biology.

The graduate student of the Department of Biochemistry should be able to practice his/her profession in a research, academic or industrial environment either in Puerto Rico or at the International level. It is expected that the graduate of the Biochemistry department contribute to the economic, social and cultural development of Puerto Rico. In order to achieve these goals the mission of the graduate program in Biochemistry is to prepare professionals with the fundamental and essential knowledge in the discipline of Biochemistry. In a wider context, the mission of the Biochemistry program is to prepare professionals that will practice their profession with the firm purpose to advance basic and applied knowledge in the field of Biochemistry, through their professional and scholarly activities contributing in solving the daily health related problems of our society which results in human benefit. It is expected that the biochemistry graduate practice their profession with the highest ethical principles, proper of the discipline they have chosen and that they set a solemn example for the future generations.

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Department of Biochemistry School of Medicine

Biochemistry

Department of Chemistry and Biochemistry | Florida …

The Department of Chemistry and Biochemistry provides students with a well-rounded education and the opportunity to participate in innovative chemical research. Our dynamic facilities and experienced faculty drivecollaborative discoveries in many fields including the chemistry of the environment, forensic chemistry, biochemistry, radiochemistry, chemistry education research and all the traditional areas of chemistry. Explore our research expertise, theFIU centers and instituteswith which we are involved, the core facilities available to us and the faculty members who make up our department.

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Biochemistry

PhD must for a prolific career in biochemistry – Times of India

Pervin Malhotra, Director, CARING Career Information & Guidance, New DelhiUnderstanding the profileTariq Ali, Bhubaneshwar: Can one get jobs in hospitals after MSc in Clinical Biochemistry?'; var randomNumber = Math.random(); var isIndia = (window.geoinfo && window.geoinfo.CountryCode === 'IN') && (window.location.href.indexOf('outsideindia') === -1 ); console.log(isIndia && randomNumber Pervin Malhotra: As careers in medical biochemistry are typically research-oriented, they require a PhD degree. The same is applicable for teaching Biochem in a medical college. After an MSc in Medical / Clinical Biochemistry you can work as a lab technician/ assistant in a hospital where you would assist in research by preparing samples, running simple tests, and communicating with doctors/scientists. Working in the field of public health or clinical research after pursuing the relevant courses are other areas besides medical transcription and coding which you could explore. Do browse through the careers section of a dozen hospital websites to see if they specifically hire MSc Biochem graduates and for which positions to get a better idea.

Options for legal practitioners

Lakshya Upreti, Kanpur: I did my LLB with a first division after BSc Chemistry. After working over a year, I now realise that I am not cut out for active legal practice. What should I do?

Pervin Malhotra: Your legal education will prove to be an asset. Having acquired a rigorous training of the mind while pursuing your legal studies, you are equipped to think logically and analytically besides being able to sharply dwell on the written and spoken word.

You can consider options like corporate law which is a hot field today, or the judicial services, the Judge Advocate General (JAG) in the Armed Forces, company secretaryship, or legal consulting as alternative options. Legal researchers are employed in large law firms and government ministries for providing legal advice. Legal Knowledge Process Outsourcing (KPO) also hire lawyers who do not wish to practice, in large numbers.

Yasmin Jehan, Aligarh:

Jessy Sam, Pune:

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PhD must for a prolific career in biochemistry - Times of India

Biochemistry

BRIEF-Lifecome Biochemistry Says The Coronavirus Outbreak Has Not Caused Significant Impact On The Company – Yahoo Singapore News

Feb 4 (Reuters) - Lifecome Biochemistry Co Ltd:

* SAYS TRANSPORTATION OF SOME RAW MATERIALS AND FINISHED PRODUCTS HAS BEEN AFFECTED DUE TO THE CORONAVIRUS OUTBREAK, BUT IT HAS NOT CAUSED SIGNIFICANT IMPACT ON THE COMPANY Source text in Chinese: https://bit.ly/2vPyW07 Further company coverage: (Reporting by Hong Kong newsroom)

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BRIEF-Lifecome Biochemistry Says The Coronavirus Outbreak Has Not Caused Significant Impact On The Company - Yahoo Singapore News

Biochemistry

Researchers Brighten Path for Creating New Type of MRI Contrast Agent – University of Texas at Dallas

UT Dallas faculty members who collaborated with Dr. Jeremiah Gassensmith (center, back), associate professor of chemistry and biochemistry, include Dr. Lloyd Lumata (left, back), assistant professor of physics, and Dr. Steven Nielsen, associate professor of chemistry. Chemistry graduate students in Gassensmiths lab include (from left, front) Oliva Brohlin, Arezoo Shahrivarkevishahi and Laurel Hagge.

University of Texas at Dallas researchers are breathing new life into an old MRI contrast agent by attaching it to a plant virus and wrapping it in a protective chemical cage.

The novel strategy is aimed at developing a completely organic and biodegradable compound that would eliminate the need to use heavy metals such as gadolinium in contrast agents, said Dr. Jeremiah Gassensmith, associate professor of chemistry and biochemistry in the School of Natural Sciences and Mathematics and corresponding author of a study published Feb. 5 in the journal Chemical Science, a publication of the Royal Society of Chemistry.

MRI is a commonly used medical imaging technology that allows physicians to see soft tissues in the body. Some tissues, like cancer, are better seen when a patient is given a contrast agent, which makes diseased parts of the body show up brightly in an MRI scan. The only class of contrast agents approved for use with MRI in the U.S. is based on the heavy metal gadolinium, which is typically excreted through a patients urine after an MRI is completed.

Because of its widespread use, gadolinium which is able to sneak through wastewater treatment plants is increasingly showing up in watersheds in and around large metropolitan areas.

Gadolinium-based contrast agents are used so much and so often that, just from patients excreting it in their urine, the metal is being released into water resources and sediments, Gassensmith said. The observed concentrations are still very low, but, nonetheless, its not exactly clear what effects long-term accumulation of gadolinium might have on the body.

In addition, for patients with compromised kidneys who have difficulty excreting these contrast agents, gadolinium can increase the risk of further kidney damage.

For these reasons, we wanted to come up with something that was biocompatible and biodegradable, something completely organic with no heavy metals, Gassensmith said.

Gassensmith and his colleagues revisited a type of organic radical contrast agent, or ORCA, that had been previously considered as an MRI contrast agent but was abandoned in part because it is not bright enough and because it is broken down too quickly in the body by ascorbate vitamin C.

This ORCA is a metal-free agent that is compatible with current MRI techniques, is less toxic to the body and is highly biodegradable. Unfortunately, on its own, its not very bright, and its so biodegradable that its impractical to use, Gassensmith said.

Gassensmiths research group repurposed the agent by first attaching the ORCA molecules to thousands of docking sites on a tobacco mosaic virus.

Since this is a plant virus, it cant infect people or animals, and its easily broken down by the liver. Because the virus is so large, it also allows us to put thousands of the ORCA molecules right next to each other, Gassensmith said. Its the difference between having one Christmas tree light, which is pretty dim, and a whole string of them together, which is quite bright.

We have some more work to do to show that our material is stable in the complex environment of the human body, and wed like to see whether we can target it to specific diseases such as cancer and other abnormalities in tissues.

Dr. Jeremiah Gassensmith, associate professor of chemistry and biochemistry at UTDallas

The researchers also had to protect the agent so that it would last long enough in the body to be practical for MRI use.

We put the ORCA in a cage, which no one had done before, Gassensmith said.

Specifically, they fabricated hollow chemical structures called cucurbiturils, so named because theyre shaped a bit like a pumpkin (from the plant family Cucurbitaceae), and wrapped them around each ORCA molecule.

The cage and the contrast agent just sort of stick together they dont form a chemical bond with one another, Gassensmith said. Its similar to the relationship between a key and a lock. Because there is no chemical bond, but the molecules stick together nonetheless, this approach is called supramolecular chemistry, which makes the agent we created a smORCA supramolecular macromolecular organic radical contrast agent.

The cage is constructed like a sieve so that water can reach the ORCA. This is necessary because MRIs use the water in the body to create an image. At the same time, the cage blocks larger molecules, like ascorbate, that can inactivate the ORCA.

In mice, the unprotected ORCA broke down within about 30 minutes, while the protected version provided more than two hours of visible contrast.

Everything we are using has been tested or part of medical research for decades. We just put them all together in a new way, Gassensmith said. We have some more work to do to show that our material is stable in the complex environment of the human body, and wed like to see whether we can target it to specific diseases such as cancer and other abnormalities in tissues.

But I think our results are a promising step toward developing smORCAs into clinically viable contrast agents.

Other UT Dallas researchers involved in the work are lead study author Hamilton Lee PhD19; chemistry graduate students Hamid Firouzi, Laurel Hagge, Arezoo Shahrivarkevishahi, Jenica Lumata, Michael Luzuriaga, Candace Benjamin and Olivia Brohlin; Christopher Parish PhD19; Dr. Steven Nielsen, associate professor of chemistry; and Dr. Lloyd Lumata, assistant professor of physics.

The research was supported by the National Science Foundation and the Welch Foundation.

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Researchers Brighten Path for Creating New Type of MRI Contrast Agent - University of Texas at Dallas