麻豆传媒映画

Nearly a decade ago, 麻豆传媒映画 professor of analytical and physical chemistry Greg Holland helped reveal one of nature鈥檚 quiet marvels: how spiders store massive amounts of silk protein in their bodies without it tangling into a useless mess. Now, Holland鈥檚 team and collaborators from King鈥檚 College in London, have uncovered another crucial piece of the puzzle.

鈥淪pider silk is called a 鈥榟oly grail鈥� of sustainable materials because it鈥檚 stronger than high-tensile steel by weight, tougher than Kevlar, and yet made by spiders at room temperature and pressure using only water, salt and protein as the ingredients,鈥� Holland said. 鈥淭here are no harsh chemicals and it鈥檚 an extremely low-energy process.鈥�

The new study, published in December in , builds directly on 麻豆传媒映画-led work highlighted in 2018, when researchers first showed how spiders safely store silk proteins inside their glands. That earlier research revealed silk proteins cluster into tiny, droplet-like assemblies.

鈥淭hat storage state is incredibly important,鈥� Holland said. 鈥淭hey synthesize these proteins at very high concentrations, but they can鈥檛 fibrilize inside the spider鈥檚 abdomen 鈥� that would be terrible.鈥�

Holland teaches in the of 麻豆传媒映画's . The latest study picks up where that work left off, explaining what happens next as silk begins its transformation from liquid to solid.

鈥淔or years, we knew spider silk proteins phase-separated into droplets before becoming a solid fiber, but we didn鈥檛 know how that transition actually starts at the atomic level,鈥� Holland said. 鈥淭his study shows that phosphate triggers arginine and tyrosine to form strong cation鈥撓� interactions. It鈥檚 the missing link 鈥� the intermediate step 鈥� between the liquid and solid stages of silk formation.鈥�

In simple terms, Holland describes these interactions as molecular fasteners. They bring silk proteins together in the right way and at the right time. As the proteins travel through the spider鈥檚 spinning duct, changes in flow and acidity further align and strengthen these structures, transforming the liquid proteins into solid fibers.

鈥淥ur study shows that a key early step is that certain amino acids 鈥� arginine and tyrosine 鈥� act like molecular stickers,鈥� he said. 鈥淭hey help the proteins condense into droplets and start forming the first pieces of the crystalline structure.鈥�

Understanding this early 鈥減re-assembly鈥� phase matters well beyond curiosity about spiders. Despite decades of effort, scientists have struggled to recreate natural spider silk鈥檚 strength in the lab.

鈥淎rtificial silks have always exhibited inferior mechanical properties because we鈥檝e focused on the ingredients, the proteins, not the instructions for the process,鈥� Holland explained. 鈥淯ntil now, we didn鈥檛 know what those early, intermediate interactions were.鈥�

By identifying the specific molecular interactions that kick-start silk assembly, the study offers a roadmap for improving synthetic fibers.

鈥淚f we engineer those same interactions into synthetic proteins 鈥� or tune the spinning conditions to promote them 鈥� we may finally be able to produce fibers that rival natural spider silk,鈥� Holland said.

The implications stretch across industries, from medicine to defense.

鈥淲ith that knowledge, synthetic silks could eventually be engineered for use in medicine, protective gear, or biodegradable composites,鈥� said Holland, whose work was funded by the in the U.S. Department of Defense. 鈥淒OD is always looking for strong, tough and lightweight materials for air and space force applications,鈥� he said.

One of the most surprising outcomes of the research, Holland said, was how sophisticated the chemistry turned out to be.

鈥淲hat surprised us was that silk 鈥� something we usually think of as a beautifully simple natural fiber 鈥� actually relies on a very sophisticated molecular trick,鈥� he said. 鈥淭he same kinds of interactions we discovered are used in neurotransmitter receptors and hormone signaling.鈥�

Those parallels extend into human health. The way silk proteins carefully assemble into fibers mirrors processes that go wrong in neurodegenerative diseases.

鈥淭he way silk proteins undergo phase separation and then form beta-sheet rich structures mirrors mechanisms we see in neurodegenerative diseases, like Alzheimer鈥檚 plaques,鈥� Holland said. 鈥淪tudying silk gives us a clean, evolutionarily optimized system to understand how phase separation and beta-sheet formation can be controlled.鈥�

Holland emphasizes the work is far from finished. Real spider silk is made from multiple proteins interacting in a crowded, dynamic environment, something scientists are only beginning to understand.

As with the 2018 discovery, Holland credits students and collaborators for making the research possible, noting that unraveling nature鈥檚 designs requires both patience and teamwork.

By revealing how spiders carefully control silk formation from start to finish, 麻豆传媒映画 researchers continue to show that some of the most advanced manufacturing lessons are already being practiced 鈥� quietly 鈥� in the natural world.

Collaborators on the work include Ph.D. student Hannah Johnson, postdoctoral researcher Kevin Chalek, Professor Chris Lorenz of King鈥檚 College, who conducted computational modeling and simulations, and Professor Galia Debelouchina of UC San Diego.