Posted on November 1, 2022 in ASRC News, Structural Biology Initiative
By Shantal Riley
The protein assembles itself into fibers spontaneously, and researchers say the results have implications for biomedicine.
The human body contains specialized tissues that need a certain amount of elasticity to function. These are incredibly important tissues found in skin, veins, arteries, and internal organs like the lungs and bladder. They owe their stretchiness to the extraordinary properties of elastin.
Elastin protein assembles into structured fibers that, along with other proteins such as collagen, give strength and flexibility to these and other tissues. Yet, exactly how this happens is not entirely understood.
In a study published last month in the Proceedings of the National Academy of Sciences, researchers set out to gain insight into this process — specifically, how elastin transforms itself from a liquid to a solid state. Using fluorescence microscopes, they observed how elastin spontaneously forms solid structures, without certain enzymes and proteins considered key for elastin assembly.
“What we saw was that there were these really small granules that were nucleating inside of the liquid,” said corresponding author Shana Elbaum-Garfinkle, an assistant professor of Biochemistry and Biology at the Graduate Center and a member of the Structural Biology Initiative at the Advanced Science Research Center.
She described this liquid stage as a dynamic phase of formation. “There was an intermediate stage where you still had a liquid and you had these little, hard granules inside of it,” she explained. “Then the liquid dissipated and these granules clustered together.”
The scientists watched the elastin assemble itself into an interconnected network of protein granules. “We were able to look through the microscope and quantify aspects of that transition in real time,” the professor said.
The study results advance the current understanding of how elastin assembles in the human body, Elbaum-Garfinkle said, and may contribute to treatments for elastin-fiber disorders such as Williams-Beuren syndrome. More directly, she said, the research may impact the design of new, elastin-inspired materials in biomedicine, including bioengineered tissues and drug delivery systems.
The study was carried out in partnership with the lab of Professor Ronald L. Koder (GC/City College, Biochemistry, Biology, Chemistry, Physics, Nanoscience). The paper’s lead author, Alfredo Vidal Ceballos, a current student in the Biochemistry Ph.D. Program at the Graduate Center, was named a 2020–2021 Art Science Connect fellow, in support of research that intersects the arts and sciences.