Writing about an extraterrestrial world full of automatons is Samantha Sylvain’s favorite pastime — when she isn’t in a lab observing protein-protein interactions.

Growing up, Sylvain knew she was going to be a scientist. She had always been interested in research and made sure to gain lab experience early, spending a large chunk of high school in the New York BioForce program. It allowed her to aid a Cornell University biophysicist in protein visualization research, igniting a passion within her for biological studies. It only made sense for her then to join Binghamton University, an R1 institute housing a First-Year Research Immersion Program that would open the door to boundless research opportunities. 

STEM wasn’t the only thing on her mind. A Queens-born poet and author, Sylvain also wanted to develop as a writer. She’s now writing a story that explores her love for scientific exploration and works to intertwine the structures of her favorite authors: William Blake and Mary Shelley.

“My story is a book of prose and poetry,” Sylvain says. “I incorporated ideas such as rebelling against rigid systems … discussed the perils of discovery and scientific innovation. I also examined the concept of technological and antiquated virtual realities.”

Sylvain believes the humanities play a large role in scientific research. She has learned to make her research accessible to groups that may be unfamiliar with scientific language, a skill she cherishes as it allows scientific discovery to become widespread. 

“You have to have a level of cognizance of how you’re writing and for what purpose,” says Sylvain, a member of the class of 2024. “You can get too fixated on writing in a specific way and structure using certain jargon — like in scientific research papers — and it can become difficult to adapt that writing style to a broader audience.” 

Her academic duality has allowed her to dive into a variety of programs on campus. Besides FRI, Sylvain was also involved in the College-in-the-Woods (CIW) Environmental Action and Studies living community, which went hand-in-hand with her McNair Scholars prospectus and her Summer Scholars and Artists Program study. Her living community’s collegiate professor — Stephen Ortiz, now the assistant vice provost for academic enrichment — became her mentor due to her involvement in so many of his realms. They’d meet weekly following the CIW sophomore colloquium, where he watched her present her study, and was in awe of her work ethic. 

“She is simply as smart, as hard-working, as thoughtful as a student can be,” Ortiz says. “I think the world of her.”

His admiration led to Ortiz recommending her to be a speaker before an audience of donors and alumni. The vice president for advancement was looking for someone who could speak to the things they’ve gotten out of Binghamton University for major benefactors, Ortiz recalls. “And in front of about 500 potential donors and alumni, she nailed it and everyone I talked to afterwards was like, ‘Thank you for bringing her to our attention, she did so awesome!’” he says. 

One of the projects Sylvain addressed during her speech was the linked work for FRI and the Summer Scholars and Artists program. Sylvain’s team conducted a study into the prevalence of the hemlock woolly adelgid (HWA), an invasive insect ravaging the Northeast. By the end of the summer, Sylvain realized in order to truly research the issue of the HWA, they would need dedicated land and more time and guidance. 

Despite the challenges she encountered, she looks at the work in a positive light. 

“That’s how I know I love research. It did infringe upon well-being and health, but I learned on the job and before the job — it was fun.” Sylvain says. “I didn’t understand that this was part of the research experience, you need to find if the project is feasible, then you can do the preliminary research, and then you figure out the larger applications. You can’t just release beetles and fungi into an area. It was very enlightening.”

She is part of biochemist Sozanne Solmaz’s lab, where she’s studying the interactions between proteins dedicated to developing the brain.

“I just fell in love with them [proteins] because I thought they were kind of cute and looked like little nanomachines that conduct various activities,” Sylvain says with a laugh. “There’s a significant amount of work that can be done to study them that relates to larger real-world issues; like neuronal migration disorders, which is the application of my research at the Solmaz lab.”  

One of Sylvain’s tasks within the project was to uncover what molecular mechanisms existed between primary proteins involved in nucleus movement during neuronal development. Through a technique used to detect physical interactions between proteins, she found that the lab’s hypothesis was correct: The proteins form spirals around one another to transport the cell nuclei.

Her next steps include an honors thesis, which will pertain to her protein research but also add in her interests within astrobiology and chemistry. 

“I’ve just begun doing research on inherently disordered proteins and how they may impact protein-protein interactions under conditions you see in extraterrestrial environments,” Sylvain says.

An Illinois native, Franks came to Binghamton University to realize her dream of living on the East Coast and her goal of becoming a doctor. Now, she’s a graduating senior majoring in biochemistry and minoring in music, finalizing her enrollment in SUNY Upstate Medical University, which she chose in part due to its proximity to an orchestra.

Her enthusiasm for research stems back to a high school experience with her older brother. Both were a part of their specialized school’s Student Inquiry and Research (SIR) program, which allowed them to collaborate with different STEM labs and health clinics. Franks worked with CRISPR/Cas9 gene editing tools and mixed lineage leukemia in breast cells. It was the project that set her on the path of cancer research.

“My brother had done the SIR program at our high school and did a really cool project about looking for differences in brain structure of those with Alzheimer’s,” Franks says. “He got to work with rat brains and present his project at conferences so I decided I wanted to do that too.”

With graduation on the horizon, Franks is focused on completing her duties in the labs where she works. At the Guthrie Clinic, she and her mentor, Gastroenterology Fellow Alex Miller, are narrowing down methods to increase the rates of hepatitis A and B vaccinations, specifically among adult patients with Chronic Liver Disease (CLD). Miller’s original goal for the project was to look at the overall population of those with CLD and to raise the vaccination rates holistically. Franks introduced the idea of finding groups within the population who may need the vaccine more urgently than others, and potentially targeting them first.

“She very thoughtfully brought in additional components that we could look at simultaneously,” Miller says. “She took us a step further and said, ‘Why don’t we introduce different types of healthcare disparities out there? That way we can see if there’s one population more vulnerable and not only increase vaccine rates but also try to focus on those in the highest need.’”

This opened the team up to looking into patient demographics, giving the researchers more insight into the types of aid and communication they would need to administer alongside the vaccination. Due to her significant contribution, Franks is in charge of data extraction for the project.

“A lot of people can learn different aspects of medicine, but what I appreciated from Miriam is that she was always willing to learn, always willing to help out however she could, and she would actively seek out tasks,” Miller says. “That’s not something that can be learned — it’s innate.”

Besides her work at Guthrie, Franks is also involved in a biochemistry lab under Susan Bane, biochemistry program director. Franks emailed her the summer before her freshman year.

“I’ve had a couple hundred undergraduate research students over the years, and never have I been contacted that early,” Bane says. “She’s planning a long way ahead and is someone who’s thought carefully about what she wants to do and the steps she needs to get there. Yet, she also focuses on what she wants to do at the moment. She isn’t doing research just to get into med school; Miriam does it because she genuinely loves it.”

In that lab, Franks is working with a partner to isolate tumor overexpressed gene (TOG) proteins from genetically modified Escherichia coli cells. They have to grow the cells themselves and then break down their membrane walls, resulting in the release of TOG protein. This is all done as a way to harvest tubulin, the main constituent of living cells’ microtubules and a primary target for many cancer medications. It’s foundational research but Bane calls it critical, as the lab had yet to attempt to collect microtubules from cancer cells.

Franks has mastered the art of splitting her attention between her two passions: research and music. When she isn’t in the lab, she’s playing the flute. She took up the instrument at age 7 and has continued to play during her college career, most notably in “The Child and the Enchantments” and “The Magic Flute.”

“I’ve been playing the flute for 16 years,” Franks says. “I started originally because my mom played the flute when she was younger so we already had one in the house. It was natural for me to follow in my mom’s footsteps so I started band in the second or third grade and I’ve been in band or orchestra ever since. I was in a few community orchestras once I got a bit older and I really found my place in it.”

Franks says she is grateful so many people at Binghamton have invested in her success. “The grad students have been amazing whenever I’m facing setbacks,” she says. “They helped me learn how to use equipment and I can ask them how to do certain equations. Of course, Dr. Bane, as well, she’s been pivotal to this entire experience. At Guthrie, working with Dr. Miller and getting to shadow him as he went through his daily tasks as a fellow really solidified for me that I want to do that, too.”

Biophysical chemist Christof Grewer is part of an eight-year collaborative project backed by a $2.4 million National Institutes of Health grant, awarded to the Icahn School of Medicine at Mount Sinai and recently renewed until 2023.

Grewer is a professor of chemistry and the department’s undergraduate program chair. He’s also one of the world’s leading researchers of glutamine, an amino acid found naturally in the body that’s critical for a healthy immune system, and ASCT2, a glutamine transporter, or the “elevator” that carries the amino acid into cells to aid in the production of proteins.

“Cancer cells become addicted to glutamine as an energy source and they import it at a very high rate, so the idea is to target and prevent the glutamine from getting to the cancer cells,” Grewer says.

Avner Schlessinger, a computational biologist and associate professor of pharmacological sciences at Mount Sinai, partnered with Grewer to develop ASCT2 inhibitors. Grewer’s lab creates compounds and oversees functional testing, while Schlessinger’s lab conducts computational analysis and predictions.

“I wanted to collaborate with Christof because he is a top expert in the world in membrane transport biophysics,” Schlessinger says. “I knew I could learn from him and work with him to test both our hypotheses. It’s an ideal collaboration because we complement each other. He is kind and patient in sharing his data and knowledge, which enables us to do better science and really have fun while doing it.”

Grewer and Schlessinger first met during a 2012 conference in Switzerland. Grewer had already established himself as an expert in membrane proteins. During his post-doctoral fellowship at Cornell University in the mid-’90s, he studied glutamate receptors — glutamate is a neurotransmitter and an important molecule in cellular metabolism — and he became a pioneer in using lasers in his research.

After seeing the similar molecular structures in glutamate and glutamine transporters and studying how glutamate transporters responded to blockers, Grewer turned his focus in 2004 to glutamine and an ASCT2 inhibitor. To date, only a handful of labs in the world are involved in similar research.

Grewer and Schlessinger published a pre-print that includes a cryo-electron microscopy structure of ASCT2 and included one of their compounds. Three of Grewer’s doctoral students have assisted in the project; Elias Ndaru was included as a pre-print author due to his instrumental and prolific work in developing compounds.

The compound synthesis and the patent application filing are only the beginning of a long research and development journey. The steps toward potential clinical applications will involve developing the next generation of compounds at ideal potency levels, extensive pre-clinical testing for efficacy and safety, and eventually clinical trials, which will require additional research and development, funding and commercialization partners, such as startups or pharmaceutical companies.

The public tends to think of cancer as one disease when in reality it’s hundreds of different diseases, Grewer says.

“We’re learning every cancer is different and there is not going to be one silver bullet to ‘cure cancer,’” he says. “There are so many molecular aspects and so many different types of tissue involved that treatment may some day be individualized to the patient.”

Grewer has been teaching at Binghamton since 2008 and is thankful to be able work with students while continuing his research. “It’s a nice balance to be in the classroom and to be able to be in the lab,” he says. “It helps me keep up with the latest technologies and developments, and I think my students benefit from that type of experience.”

At Binghamton University, Susan Bane thinks she’s found an answer: an ADC that uses a boronic acid to bind cancer-fighting drugs to the proteins on the surface of cancer cells, creating a chemical reaction that could be well-suited for drug delivery, with the potential to avoid the complications of chemotherapy and radiation.

“Killing non-cancer cells is where side effects come from, which is why this research is so important to pharmaceutical companies,” says Bane, a professor of organic and biological chemistry who received a $50,000 investment from the SUNY Technology Accelerator Fund (TAF) in June. “You can make antibodies that recognize very, very specific things on the surface of cancer cells, things that are in much higher abundance than they are on a normal cell. These antibodies can attach themselves to the cancers, making the specific bonds that you want to see between the drug and the antibody. There aren’t a lot of chemistries that can make that happen efficiently, but we believe this method will be fast enough to use in a clinical setting.”

For the past 30 years, Bane’s cancer work has focused on microtubules, intracellular structures that are involved in cell division and organization. In this most recent breakthrough, she was conducting basic research on microtubules, trying to speed up a chemical reaction, and decided to add boron. Bane expected the reaction to take hours; instead, it finished within seconds, providing an a-ha moment that pushed her research into a new direction.

“We found it by accident, while were working on a completely different project,” Bane says. “We thought that if we tried the reaction with boronic acid, we could make it faster. Not only did we make it faster, we made it thousands of times faster. We thought, ‘What just happened?’ Chemists had made these kinds of molecules before, using a much slower process, but our pieces just snapped together. We were completely blown away, and that’s how we ended up here.”

The result of this latest research, patented as “Rapid and efficient bioorthogonal ligation reaction and boron-containing heterocycles useful in conjunction therewith,” has distinct advantages over products currently on the market. First, there’s speed, which should make the molecule much easier to produce and much quicker to react. Second, its reagents are more biocompatible, so there aren’t any concerns about its toxicity in the human body. Third, it’s able to work well in water, even at highly diluted levels, and can be used without having to eliminate excess reagents after treatment.

Like other bioorthogonal chemical reactions, which are increasingly being used in personalized medicine, Bane’s product can be carefully controlled for consistency. Plus, this same patented process has potential applications in medical imaging, where it could create radioactive molecules to make PET scans safer, more efficient and less expensive.

“We think this reaction has a lot of potential utilities, and we’re interested in seeing where it can go,” Bane says. “One step is to reach across the academic community, let people know about our work and find out where they can take it. Another is to move outside academia, to places that have the resources to develop this. We’re at the stage now where we want to show this process can work on a larger scale and in a more controlled environment. But first, we have to get this into the hands of people with enough resources to take it to the next step.”

That’s where SUNY’s Technology Accelerator Fund comes in. To bring the patent closer to clinical trials, Bane is using her investment to manufacture experimental quantities of the novel chemical reagents and modified antibodies, purchase the commercial material currently available and begin testing the two head-to-head in her Binghamton laboratory. At the same time, she has begun leasing the technology to outside labs, where it’s being tested for a variety of potential biomedical and pharmaceutical applications.

“The more material that gets out there, the more people will be doing basic research, the more peer-reviewed publications we’ll have and the more interest will be generated for this type of chemistry,” Bane says. “Drug development is enormously expensive for pharmaceutical companies, and before we can find investors, we need to show that this process will work in a much more controlled environment. TAF is helping us reach the stage where our product will be more attractive to potential licensees, including the companies that could ultimately develop this for the marketplace. Getting the TAF grant is showing people that this project has commercial viability.”

Binghamton University biochemist Brian Callahan has discovered a new way to fight cancer, one that attacks only the cancer cells and promises fewer side effects.

He hunts hedgehogs. No, he’s not Elmer Fudd.

Hedgehogs are proteins that help govern how cells develop. Normally, once a person reaches maturation, the hedgehogs turn off. But in some cancers — prostate, pancreatic, ovarian and lung in particular — the hedgehogs somehow turn back on, and force uncontrolled cell growth: cancer.

“Pharmaceutical companies have been after hedgehogs for years,” says Callahan, an assistant professor of biological chemistry. One in particular, Erivedge, binds with the same receptors that hedgehogs activate, blocking the cancer development.

“We don’t want to compete with Big Pharma,” Callahan says. “We’re trying a new strategy; we’re going after hedgehogs directly.”

Callahan recently published two papers, one about zinc and hedgehogs in the May edition of the Journal of Biological Chemistry, and one about phenylarsine oxide in the January edition of Chembiochem, in partnership with researchers from Rensselaer Polytechnic Institute.

Both substances don’t simply block hedgehog reception; they shut hedgehogs down, preventing inactive hedgehogs from becoming biologically active and causing malignancies.

But before you start sucking on pennies or drinking phenylarsine oxide — an arsenic compound that will pretty effectively ruin your liver and kidneys — keep in mind that Callahan hasn’t discovered the medicine, just the method.

“It’s a proof of concept,” he says of his Department of Defense-funded work. “We can, with a small molecule, prevent the hedgehog from functioning. We think they bind a little differently. The arsenic seems to bind more tightly; it seems to be much more potent.”

The next step is a partnership with Michelle Arkin, an associate professor at the University of California San Francisco’s School of Pharmacy. During the next year or so, her lab will mirror Callahan’s first experiments with 80,000 or so compounds in its library.

“We’re looking for molecules that inhibit the functions that Brian found,” Arkin says. She expects a hit rate of between 0.1 percent and 0.5 percent — or maybe 100 or 200 compounds.

“There will be a lot of chemistry, a lot of tweaking,” Arkin says. “What we’ll get out of this is a puzzle piece,” an idea of a molecule that disrupts the hedgehogs without causing undue side effects.

The best candidates will be tested in lab animals, probably sometime in 2017, Callahan says. After that? It’s a matter of where the science leads.

“We want to get to molecularly targeted therapy,” Callahan says. In essence, a magic bullet that kills the cancer and not the patient.

Callahan does warn of one unavoidable side effect, though: Hedgehogs also govern hair growth. Turn them off, and the patient’s hair will fall out. Wascally hedgehogs.