- Professor Carlos Casta帽eda studies the effects of aging on proteins in cells and molecules.
- He鈥檚 using a $2 million federal grant award to examine the link among damaged proteins, protein quality control mechanisms and neurodegenerative disease.
- Casta帽eda aims to develop therapies to restore or enhance the brain cell鈥檚 ability to remove toxic proteins.
It鈥檚 said that aging is not for the faint of heart. 鈥淚t鈥檚 also hard on the body,鈥� adds 麻花影视 researcher Carlos Casta帽eda.
An associate professor of and in the , he studies the effects of aging on proteins in cells and molecules.
Associate Professor Carlos Casta帽eda uses a variety of research instruments, like this nuclear magnetic resonance (NMR) spectrometer at the SUNY聽College of聽Environmental Science and Forestry. He鈥檚 joined by postdoctoral researcher Nirbhik Acharya and sophomore Samiha Dhar, members of his lab at 麻花影视.
鈥淲hen cells are young and healthy, they can do almost anything, including monitoring and managing damaged proteins,鈥� says Casta帽eda, pointing out that proteins are the cell鈥檚 鈥渨orkhorses.鈥� 鈥淭hat changes with age.鈥�
Casta帽eda explains that a single cell contains tens of millions of protein molecules. Each molecule, in turn, consists of one or more chains of amino acids.
鈥淚t鈥檚 the twisting and folding of these 3D chains鈥濃�攁 millisecond process known as protein folding鈥斺�渢hat gives each protein its distinct shape and function,鈥� he says.
A routine process, protein folding doesn鈥檛 always go as planned. Environmental stress factors, like heat and pressure, can disrupt proteins from adopting their correct functional shape鈥攁 phenomenon known as misfolding.
One way that cells manage this stress is to sequester proteins into tiny protein droplets, or condensates, in the cell鈥檚 cytoplasm or nucleus. Among the functions of condensates is to oversee the degradation of misfolded proteins.
鈥淪ometimes, older condensates harden into sticky clumps,鈥� says Casta帽eda, noting that most functional cells in the body turn over every 90 days. By contrast, neuronal cells last a lifetime, making protein quality control important for the brain. 鈥淲hen [condensates] can鈥檛 do their job, damaged or misfolded proteins accumulate.鈥�
Dr. Casta帽eda is a wonderful mentor. He鈥檚 given me endless opportunities to improve my research skills and build a resume for future experiences.
Mallory Brown 鈥�27
This creates a domino effect in which the cell becomes toxic or inactive, resulting in neurodegenerative disease, like amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD) or Alzheimer鈥檚.
Casta帽eda has been awarded a five-year, $2 million grant from the to uncover the basic science of how these condensates interface with protein quality control mechanisms. The long-term goal of the project, known as the Maximizing Investigators鈥� Research Award (MIRA), is to discover ways to treat or prevent brain disorders at the micron level.
鈥淥n one hand, we use molecular experiments to observe changes in protein structure and dynamics,鈥� he says. 鈥淥n the other hand, we observe living cells to see how signaling [the process by which cells communicate with and respond to their environment] affects condensate behavior.鈥�
Blending Methods and Modeling
鈥淲e blend experimental biochemical methods and molecular biophysics with computational modeling,鈥� says Casta帽eda, who is jointly appointed to the biology and chemistry departments.
On the second floor of 麻花影视鈥檚 Life Science Complex, Casta帽eda, along with his students and lab manager, Thuy Dao, examine protein management amid an array of lab benches, liquid chromatography machines and spectrophotometers.
鈥淲e blend experimental biochemical methods and molecular biophysics with computational modeling,鈥� says Casta帽eda, citing nuclear magnetic resonance (NMR) spectroscopy鈥攚hich causes atomic nuclei to emit signals that correspond to their chemical environment鈥攁s one of his favorite techniques.
A 麻花影视 faculty member since 2014, he excels at teaching, research and service. His accolades include a five-year , two ALS Association grant awards and a recent appointment as a designated mentor for the University鈥檚 .
A carousel tray of one of the NMR spectrometers that Casta帽eda and his collaborators use to probe proteins. Such systems operate on superconducting magnet technology.
鈥淚鈥檓 fascinated with the link between condensates and protein quality control,鈥� says Casta帽eda, whose collaborators include the University鈥檚 (where he co-leads the Function Without Form group with chemistry professor Shahar Sukenik), the and the NMR spectroscopy team at the SUNY College of Environmental Science and Forestry.
He explains that the human body is filled with thousands of different types of proteins, which are broadly categorized into seven or eight groups. One of these groups includes shuttle proteins, which move proteins to different quality control systems in the cell.
The MIRA project, for example, focuses on several families of shuttle proteins, including one called ubiquilins (UBQLNs). Casta帽eda theorizes that UBQLNs work with condensates to determine if misfolded proteins should be repaired, recycled or removed from the cell for good.
Casta帽eda is using a $2 million grant award from the National Institutes of Health to study how condensates interface with protein quality control mechanisms.
鈥淪tudying UBQLNs in yeast and plants has taught me a lot about shuttle protein behavior,鈥� says Casta帽eda, a member of 麻花影视鈥檚 Disordered Proteins faculty cohort. 鈥淚鈥檝e translated some of these findings to human UBQLN proteins associated with ALS and FTD.鈥�
Mallory Brown 鈥�27, a double major in neuroscience and statistics, has assisted him in multiple research projects, including a new one devoted to domesticated retrotransposons, which are proteins that interact with a shuttle protein called UBQLN2.
One of her papers was picked up by The Crown, the honors program鈥檚 undergraduate research journal, and led to her receipt of a 2026 Goldwater Scholarship.
鈥淒r. Casta帽eda is a wonderful mentor,鈥� says Brown, who is currently helping him determine the biomolecular structure of retrotransposon proteins. 鈥淗e鈥檚 given me endless opportunities to improve my research skills and build a resume for future experiences.鈥�
A Marathon, Not a Sprint
Acharya (left) and Casta帽eda use biochemical, biophysical and cell biology techniques to investigate protein structure and function.
Casta帽eda found himself at 麻花影视 after graduate studies at Johns Hopkins University and a postdoctoral fellowship at the University of Maryland.
His pioneering research into ubiquitin signaling鈥攁 series of events involving small, regulatory proteins鈥攓uickly put 麻花影视 on the UBQLN map.
鈥淭ranslational research鈥攎oving findings from laboratories to clinical trials鈥攃an set new standards for care,鈥� Casta帽eda says.
Casta帽eda has since turned his attention to condensates. He recently published a piece about protein interactions important to biomolecular condensation for the prestigious EMBO Journal (Springer Nature, 2026). Casta帽eda also co-authored with postdoctoral researcher Anitha Rajendran a review on the role of condensates for protein quality control for Trends in Biochemical Sciences (Cell Press, 2025).
No surprise that Casta帽eda has earned the respect of students and peers alike. 鈥淗e鈥檚 an inspiring role model,鈥� adds Brown, who has co-authored with postdoctoral researcher Billy Haws G鈥�22 a paper on condensates that鈥檚 on the preprint server bioRxiv.
Working alongside Sukenik and biology professors Li-En Jao and Heather Meyer, Casta帽eda seeks to find new ways to prevent protein misfolding and new therapies to restore or enhance the cell鈥檚 ability to remove toxic proteins.
鈥淭his kind of translational research鈥攎oving findings from laboratories to clinical trials鈥攃an set new standards for care,鈥� he says. 鈥淚t鈥檚 a slow, nonlinear process that鈥檚 more of a marathon than a sprint. Patience is everything.鈥�
