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 一頭牛日式燒肉值得排隊嗎？》公益路10大美食推薦｜從燒肉到火鍋全攻略 |
| 興趣嗜好｜偶像追星 2026/04/20 10:43:58 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
身為一個熱愛美食、喜歡在城市裡挖掘驚喜的人，臺中公益路一直是我最常出沒的地方之一。這條路可說是「臺中人的美食戰場」，從精緻西餐到創意火鍋，從日式丼飯到義式早午餐，每走幾步，就會有完全不同的特色料理餐廳。 這次我特別花了一整個月，實際造訪了公益路上十間口碑不錯的餐廳。有的是網友熱推的打卡名店，也有隱藏在巷弄裡的小驚喜。我以環境氛圍、口味表現、價格CP值與再訪意願為基準，整理出這篇實測評比。希望能幫正在猶豫去哪裡吃飯的你，找到那一間「吃完會想再來」的餐廳。 評比標準與整理方向
這次我走訪的10家餐廳橫跨不同料理類型，從高質感牛排館到巷弄系早午餐，每一間都有自己獨特的風格。為了讓整體比較更客觀，我依照以下四大面向進行評比，並搭配實際用餐體驗來打分。
整體而言，我希望這份評比不只是「哪家好吃」，而是幫你在不同情境下（約會、家庭聚餐、朋友小聚、商業午餐）都能快速找到合適的選擇。畢竟，美食不只是味覺的滿足，更是一段段與朋友共享的生活記憶。 10間臺中公益路餐廳評比懶人包公益路向來是臺中人聚餐的首選地段，從火鍋、燒肉到中式料理與早午餐，每走幾步就有驚喜。以下是我實際造訪過的10間代表性餐廳清單，橫跨平價、創意、高級各路風格。
一頭牛日式燒肉｜炭香濃郁的和牛饗宴，約會聚餐首選
走在公益路上，很難不被 一頭牛日式燒肉 的木質外觀吸引。低調卻不失質感的門面，搭配昏黃燈光與暖色調的內裝，讓人一進門就感受到濃濃的日式職人氛圍。店內空間不大，但桌距規劃得宜，每桌皆設有獨立排煙設備，烤肉時完全不怕滿身油煙味。 餐點特色
一頭牛的靈魂，絕對是他們招牌的「三國和牛拼盤」。 用餐體驗整體節奏掌握得非常好。店員會在你剛想烤下一片肉時貼心遞上夾子、幫忙換烤網，讓人完全不用分心。整場用餐過程就像一場表演，從視覺、嗅覺到味覺都被滿足。 綜合評分
地址：408臺中市南屯區公益路二段162號電話：04-23206800 小結語一頭牛日式燒肉不僅是「吃肉的地方」，更像是一場五感盛宴。從進門那一刻到最後一道甜點，都能感受到他們對細節的用心。 TANG Zhan 湯棧｜文青系火鍋代表，麻香湯底與視覺美感並重
在公益路這條美食戰線上，TANG Zhan 湯棧 是讓人一眼就會想走進去的那一種。 餐點特色
湯棧最有名的當然是它的「麻香鍋」。 用餐體驗整體氛圍比一般火鍋店更有質感。 綜合評分
地址：408臺中市南屯區公益路二段248號電話：04-22580617 官網：https://www.facebook.com/TangZhan.tw/ 小結語TANG Zhan 湯棧 把傳統火鍋做出新的樣貌保留臺式鍋物的溫度，又結合現代風格與細節服務，讓吃鍋這件事變得更有品味。 如果你想找一間兼具「好吃、好拍、好放鬆」的火鍋店，湯棧會是公益路上最有風格的選擇之一。 NINI 尼尼臺中店｜明亮寬敞的義式早午餐天堂
如果說前兩間是肉食愛好者的天堂，那 NINI 尼尼臺中店 絕對是想放鬆、聊聊天的好地方。餐廳外觀以白色系與大片玻璃窗為主，陽光灑進室內，讓人一踏入就有種度假般的輕盈感。假日早午餐時段特別熱鬧，建議提早訂位。 餐點特色
NINI 的菜單融合義式與臺灣人口味，選擇多樣且份量十足。主打的 松露燉飯 濃郁卻不膩口，米芯保留微Q口感；而 香蒜海鮮義大利麵 則以新鮮白蝦、花枝與淡菜搭配微辣蒜香，口感層次豐富。 用餐體驗店內氣氛輕鬆不拘謹，無論是一個人帶電腦工作、或朋友聚餐，都能找到舒服角落。餐點上桌速度穩定，服務人員態度親切、補水與收盤都非常主動。整體節奏讓人覺得「時間變慢了」，很適合想遠離忙碌日常的人。 綜合評分
地址：40861臺中市南屯區公益路二段18號電話：04-23288498 小結語NINI 尼尼臺中店是一間能讓人放下手機、慢慢吃飯的餐廳。餐點不追求浮誇，而是以「剛剛好」的份量與風味，陪伴每個平凡午後。如果你在找一間能邊吃邊聊天、拍照也漂亮的早午餐店，NINI 會是你在公益路上最不費力的幸福選擇。 加分100%浜中特選昆布鍋物｜平價卻用心的湯頭系火鍋，家庭聚餐好選擇
在公益路這條高質感餐廳林立的戰場上，加分100%浜中特選昆布鍋物 走的是截然不同的路線。它沒有浮誇的裝潢、也沒有高價位的套餐，但靠著實在的湯頭與親切的服務，默默吸引許多回頭客。每到用餐時間，總能看到家庭或情侶三兩成群地圍著鍋邊聊天。 餐點特色
主打 北海道浜中昆布湯底，湯頭清澈卻不單薄，越煮越能喝出海藻與柴魚的自然香氣。 用餐體驗整體氛圍偏家庭取向，桌距寬敞、座位舒適，帶小孩來也不覺擁擠。店員態度親切，補湯、收盤都很勤快，給人一種「被照顧著」的安心感。 綜合評分
地址：403臺中市西區公益路288號電話：0910855180 小結語加分100%浜中特選昆布鍋物是一間「不浮誇、但會讓人想再訪」的火鍋店。它不追求豪華擺盤，而是用最簡單的湯頭與新鮮食材，傳遞出家常卻不平凡的溫度。 印月餐廳｜中式料理的藝術演繹，宴客與家庭聚會首選
說到臺中公益路的中式料理代表，印月餐廳 絕對是榜上有名。這間開業多年的餐廳以「中菜西吃」的概念聞名，把傳統中式料理以現代手法重新詮釋。從建築外觀到餐具擺設，每個細節都散發著低調的典雅氣息。 餐點特色
印月最令人印象深刻的是他們將傳統中菜融入創意手法。 用餐體驗服務方面完全對得起餐廳的高級定位。從入座、點餐到上菜節奏，都拿捏得恰如其分。每道菜都會有服務人員細心介紹食材與吃法，讓人感受到「被款待」的尊榮感。 綜合評分
地址：408臺中市南屯區公益路二段818號電話：0422511155 小結語印月餐廳是一間「不只吃飯，更像品味生活」的地方。 KoDō 和牛燒肉｜極致職人精神，專為儀式感與頂級味覺而生
若要形容 KoDō 和牛燒肉 的用餐體驗，一句話足以總結——「像在欣賞一場關於肉的表演」。 餐點特色
這裡主打 日本A5和牛冷藏肉，以「精切厚燒」的方式呈現。 用餐體驗KoDō 的最大特色是「儀式感」。 綜合評分
地址：403臺中市西區公益路260號電話：0423220312 官網：https://www.facebook.com/kodo2018/ 小結語KoDō 和牛燒肉不是日常餐廳，而是一場體驗。 永心鳳茶｜在茶香裡用餐的優雅時光，臺味早午餐的新詮釋
走進 永心鳳茶公益店，彷彿進入一間有氣質的茶館。 餐點特色
永心鳳茶的餐點結合中式靈魂與西式擺盤，無論是「炸雞腿飯」還是「紅玉紅茶拿鐵」，都能讓人感受到熟悉卻不平凡的味道。 用餐體驗店內服務人員態度溫和，對茶品介紹詳盡。上餐節奏剛好，不急不徐。 綜合評分
地址：40360臺中市西區公益路68號三樓(勤美誠品)電話：0423221118 小結語永心鳳茶讓人重新定義「臺味」。 三希樓｜老饕級江浙功夫菜，穩重又帶人情味的中式饗宴
位於公益路上的 三希樓 是許多臺中老饕的口袋名單。 餐點特色
三希樓的菜色以 江浙與港式料理 為主，兼顧傳統與現代風味。 用餐體驗三希樓的服務給人一種老派但貼心的感覺。 綜合評分
地址：408臺中市南屯區公益路二段95號電話：0423202322 官網：https://www.sanxilou.com.tw/ 小結語三希樓是一間「吃得出功夫」的餐廳。 一笈壽司｜低調奢華的無菜單日料，職人手藝詮釋旬味極致
在熱鬧的公益路上，一笈壽司 低調得幾乎不顯眼。 餐點特色
一笈壽司採 Omakase（無菜單料理） 形式，每一餐都由主廚根據當日食材設計。 用餐體驗整場用餐約90分鐘，節奏緩慢但沉穩。 綜合評分
地址：408臺中市南屯區公益路二段25號電話：0423206368 官網：https://www.facebook.com/YIJI.sushi/ 小結語一笈壽司是一間真正讓人「放慢呼吸」的餐廳。 茶六燒肉堂｜人氣爆棚的和牛燒肉聖地，肉香與幸福感同時滿分
若要票選公益路上「最難訂位」的餐廳，茶六燒肉堂 絕對名列前茅。 餐點特色
茶六主打 和牛燒肉套餐，價格約落在 $700–$1000 間，份量與品質兼具。 用餐體驗茶六的服務效率相當高。店員親切、換網勤快、補水速度快，整場用餐流程流暢無壓力。 綜合評分
地址：403臺中市西區公益路268號電話：0423281167 官網：https://inline.app/booking/-L93VSXuz8o86ahWDRg0:inline-live-karuizawa/-LUYUEIOYwa7GCUpAFWA 小結語茶六燒肉堂用「穩定品質＋輕奢氛圍」抓住了臺中年輕族群的心。 吃完10家公益路餐廳後的心得與結語吃完這十家餐廳後，臺中公益路不只是一條美食街，而是一段生活風景線。 有的餐廳講究細膩與儀式感，像 一頭牛日式燒肉 與 一笈壽司，讓人感受到食材最純粹的美好 有的則以親切與溫度打動人心，像 加分昆布鍋物、永心鳳茶，讓人明白吃飯不只是為了飽足，而是一種被照顧的幸福。 而像茶六燒肉堂、TANG Zhan 湯棧 這類人氣名店，則用穩定的品質與熱絡的氛圍，成為許多臺中人心中「想吃肉就去那裡」的代名詞。 這十家店，構成了公益路最動人的縮影 有華麗的，也有溫柔的；有傳統的，也有創新的。 每一家都在自己的風格裡發光，讓人吃到的不只是料理，而是一種生活的溫度與節奏。 對我而言，這不僅是一場美食旅程，更是一趟關於「臺中味道」的回憶之旅。 FAQ：關於臺中公益路美食常見問題Q1：公益路哪一區的餐廳最集中？ Q2：需要提前訂位嗎？ 最後的話若要用一句話形容這趟美食之旅，我會說： 一笈壽司尾牙拍照效果好嗎？ 如果你也和我一樣喜歡用味蕾探索一座城市，那就把這篇公益路美食攻略收藏起來吧。三希樓適合多人分享嗎？ 無論是約會、慶生、家庭聚餐，或只是想犒賞一下辛苦的自己——這條路上永遠會有一間剛剛好的餐廳在等你。TANG Zhan 湯棧適合辦尾牙嗎？ 下一餐，不妨從這10家開始。一笈壽司單點比較好嗎？ 打開手機、約上朋友，讓公益路成為你生活裡最容易抵達的小確幸。TANG Zhan 湯棧春酒場面夠體面嗎？ 如果你有私心愛店，也歡迎留言分享，茶六燒肉堂有雷嗎？ 你的推薦，可能讓我下一趟美食旅程變得更精彩。三希樓值得專程去嗎？ Scientists have discovered a mechanism to prevent darkening and health risks in cold-stored potatoes, a breakthrough promising healthier, tastier snacks and addressing a billion-dollar market’s challenges. Their work, revealing a gene responsible for cold-induced sweetening (CIS), could lead to new potato varieties that avoid acrylamide formation, benefiting the snack food industry and potentially reducing food waste and costs. Researchers at Michigan State University have discovered a method to decrease the levels of a carcinogen generated during the frying of tubers that have been stored in cold conditions. In a breakthrough for the snack food industry, a team of scientists led by Michigan State University professors Jiming Jiang and David Douches has discovered a key mechanism behind the darkening and potential health concerns associated with cold-stored potatoes. Their findings, published in the journal The Plant Cell, hold promise for the development of potato varieties that could be stored under cold temperatures and lead to healthier and tastier chips and fries. These snacks have a market worth billions of dollars in the U.S. In Michigan — the nation’s leading producer of potatoes for chips — the potato industry is valued at $240 million annually. Michigan State University researchers David Douches (left) and Jiming Jiang (right) work with potato plants in Michigan State University’s Agronomy Farm Greenhouse. Credit: Paul Henderson/MSU But farmers can’t grow the crops year-round and snack makers need a constant supply of fresh spuds to meet their demands. Preserving potatoes in cold storage ensures chip and fry producers have what they need, but the low temperatures also trigger a process called cold-induced sweetening, or CIS, which converts starches to sugars. Processing tubers loaded with sugars results in darkened fries and chips. It also generates acrylamide, a carcinogenic compound formed during high-temperature processing, which has been linked to health concerns including an increased cancer risk. Although there are techniques to reduce sugars in cold-stored tubers, these add cost and can affect the flavor of the final product. So Jiang and his colleagues have focused on the root of the problem to work toward potatoes that aren’t affected by CIS, to begin with. “We’ve identified the specific gene responsible for CIS and, more importantly, we’ve uncovered the regulatory element that switches it on under cold temperatures,” explained Jiang, an MSU Research Foundation Professor in the departments of Plant Biology and Horticulture. “By studying how this gene turns on and off, we open up the possibility of developing potatoes that are naturally resistant to CIS and, therefore, will not produce toxic compounds.” By switching off the potato vacuolar invertase gene, or VInv, Michigan State University researchers have shown that frying potatoes stored at cold temperatures can result in a healthier and more appealing chip. Credit: Adapted from Bhaskar, P.B., et al. Plant Physiology, 2010, 154 (2), 939–948, https://doi.org/10.1104/pp.110.162545 From lab, to greenhouse, to chip bag Jiang, a potato researcher for over 20 years, has dedicated his career to solving this puzzle. To overcome one of the most pressing issues in the potato industry, Jiang started his work to minimize acrylamide in potato chips and fries at the University of Wisconsin-Madison. There, Jiang and his team published a paper in 2010 identifying a key gene responsible for potato CIS. Moving to MSU in 2017, Jiang and his team have worked to pinpoint which elements of that gene could be modified to stop the process of cold-induced sweetening. Jiang’s research team, which includes collaborators across MSU’s campus as well as at other research universities, used a combination of gene expression analysis, protein identification, and enhancer mapping to pinpoint the regulatory element controlling the CIS gene. “MSU’s collaborative research environment and facilities, including the world-class potato breeding program led by Dave Douches, were instrumental for this research,” Jiang said. “Our next steps involve using this knowledge to create CIS-resistant potato lines through gene editing or other breeding techniques in Dr. Douches’ greenhouses.” Researchers are growing healthier, more snackable potatoes in Michigan State University’s Agronomy Farm Greenhouse. Credit: Paul Henderson/MSU The lead of the MSU Potato Breeding and Genetics Program, Douches put into practice a technique Jiang developed to stop CIS through gene editing. “All our facilities are on campus so the research work can be done efficiently,” Douches said. “With our collaboration, we were able to produce a finding that paves the way for targeted genetic modification approaches to create cold-resistant potato varieties.” The potential benefits of this research extend beyond improved snack food quality. Reducing acrylamide formation in potatoes could have implications for other processed starchy foods. Additionally, cold-resistant potatoes could offer greater flexibility in storage and transportation, potentially reducing food waste and costs. Jiang believes the new CIS-resistant potatoes could be commercially available in the near future. “This discovery represents a significant advancement in our understanding of potato development and its implications for food quality and health,” Jiang said. “It has the potential to affect every single bag of potato chips around the world.” Reference: “Molecular dissection of an intronic enhancer governing cold-induced expression of the vacuolar invertase gene in potato” by Xiaobiao Zhu, Airu Chen, Nathaniel M Butler, Zixian Zeng, Haoyang Xin, Lixia Wang, Zhaoyan Lv, Dani Eshel, David S Douches and Jiming Jiang, 20 February 2024, The Plant Cell. DOI: 10.1093/plcell/koae050 We have long known that biological materials absorb ambient moisture. But new research from Columbia shows that ambient water is much more central to the character of natural materials such as pine cones, fungi, and other plants and trees than was previously known. A recent study argues that materials like wood, bacteria, and fungi belong to a newly identified class of matter, “hydration solids.” For many years, the fields of physics and chemistry have held the belief that the properties of solid materials are fundamentally determined by the atoms and molecules they consist of. For instance, the crystalline nature of salt is credited to the ionic bond formed between sodium and chloride ions. Similarly, metals such as iron or copper owe their robustness to the metallic bonds between their respective atoms, and the elasticity of rubbers stems from the flexible bonds in the polymers that form them. This principle also applies to substances like fungi, bacteria, and wood. Or so the story goes. A new paper recently published in Nature upends that paradigm, and argues that the character of many biological materials is actually created by the water that permeates these materials. Water gives rise to a solid and goes on to define the properties of that solid, all the while maintaining its liquid characteristics. In their paper, the authors group these and other materials into a new class of matter that they call “hydration solids,” which they say “acquire their structural rigidity, the defining characteristic of the solid state, from the fluid permeating their pores.” The new understanding of biological matter can help answer questions that have dogged scientists for years. “I think this is a really special moment in science,” Ozgur Sahin, a professor of Biological Sciences and Physics and one of the paper’s authors, said. “It’s unifying something incredibly diverse and complex with a simple explanation. It’s a big surprise, an intellectual delight.” The new findings emerged from Professor Sahin’s ongoing research into the strange behavior of spores, dormant bacterial cells, shown here. Credit: Xi Chen Steven G. Harrellson, who recently completed doctoral studies in Columbia’s physics department, and is an author on the study, used the metaphor of a building to describe the team’s finding: “If you think of biological materials like a skyscraper, the molecular building blocks are the steel frames that hold them up, and water in between the molecular building blocks is the air inside the steel frames. We discovered that some skyscrapers aren’t supported by their steel frames but by the air within those frames.” “This idea may seem hard to believe, but it resolves mysteries and helps predict the existence of exciting phenomena in materials,” Sahin added. When water is in its liquid form, its molecules strike a fine balance between order and disorder. But when the molecules that form biological materials combine with water, they tip the balance toward order: Water wants to return to its original state. As a result, the water molecules push the biological matter’s molecules away. That pushing force, called the hydration force, was identified in the 1970s, but its impact on biological matter was thought to be limited. This new paper’s argument that the hydration force is what defines the character of biological matter almost entirely, including how soft or hard it is, thus comes as a surprise. We have long known that biological materials absorb ambient moisture. Think, for example, of a wooden door, that expands during a humid spell. This research, however, shows that ambient water is much more central to wood, fungi, plants, and other natural materials’ character than we had ever known. A Simple Mathematical Framework for Complex Properties The team found that bringing water to the front and center allowed them to describe the characteristics that familiar organic materials display with very simple math. Previous models of how water interacts with organic matter have required advanced computer simulations to predict the properties of the material. The simplicity of the formulas that the team found can predict these properties suggests that they’re onto something. Spirit Island, Jasper National Park, Canada. “When we take a walk in the woods, we think of the trees and plants around us as typical solids,” Professor Ozgur Sahin said. “This research shows that we should really think of those trees and plants as towers of water holding sugars and proteins in place.” Credit: Terry Ott To take one example, the team found that the simple equation E=Al/λ neatly describes how a material’s elasticity changes based on factors including humidity, temperature, and molecule size. (E in this equation refers to the elasticity of a material; A is a factor that depends on the temperature and humidity of the environment; l is the approximate size of biological molecules and λ is the distance over which hydration forces lose their strength). “The more we worked on this project, the simpler the answers became,” Harrellson said, adding that the experience “is very rare in science.” The new findings emerged from Professor Sahin’s ongoing research into the strange behavior of spores, dormant bacterial cells. For years, Sahin and his students have studied spores to understand why they expand forcefully when water is added to them and contract when water is removed. (Several years ago, Sahin and colleagues garnered media coverage for harnessing that capability to create small engine-like contraptions powered by spores.) Around 2012, Sahin decided to take a step back to ask why the spores behave the way they do. He was joined by researchers Michael S. DeLay and Xi Chen, authors on the new paper, who were then members of his lab. Their experiments did not provide a resolution to the mysterious behavior of spores. “We ended up with more mysteries than when we started,” Sahin remembers. They were stuck, but the mysteries they encountered were hinting that there was something worth pursuing. After years of pondering potential explanations, it occurred to Sahin that the mysteries the team continually encountered could be explained if the hydration force governed the way that water moved in spores. The team had to do more experiments to test the idea. In 2018, Harrellson, who is now a software engineer at the data analytics firm Palantir, joined the project. From Complexity to Simplicity “When we initially tackled the project, it seemed impossibly complicated. We were trying to explain several different effects, each with their own unsatisfying formula. Once we started using hydration forces, every one of the old formulas could be stripped away. When only hydration forces were left, it felt like our feet finally hit the ground. It was amazing, and a huge relief; things made sense,” he said. The results of those experiments led the team and their collaborators to this paper. In addition to Harrellson, DeLay, Chen, and Sahin, the paper’s other authors are Ahmet-Hamdi Cavusoglu, Jonathan Dworkin, and Howard A. Stone. Adam Driks of Loyola University Chicago, who also contributed research, passed away before the completion of the work. The paper’s findings apply to huge amounts of the world around us: Hygroscopic biological materials–that is, biological materials that allow water in and out of them–potentially make up anywhere from 50% to 90% of the living world around us, including all of the world’s wood, but also other familiar materials like bamboo, cotton, pine cones, wool, hair, fingernails, pollen grains in plants, the outer skin of animals, and bacterial and fungal spores that help these organisms survive and reproduce. The term coined in the paper, “hydration solids,” applies to any natural material that’s responsive to the ambient humidity around it. With the equations that the team identified, they and other researchers can now predict materials’ mechanical properties from basic physics principles. So far that was true mainly of gases, thanks to the well-known general gas equation, which has been known to scientists since the 19th century. “When we take a walk in the woods, we think of the trees and plants around us as typical solids. This research shows that we should really think of those trees and plants as towers of water holding sugars and proteins in place,” Sahin said: “It’s really water’s world.” Reference: “Hydration solids” by Steven G. Harrellson, Michael S. DeLay, Xi Chen, Ahmet-Hamdi Cavusoglu, Jonathan Dworkin, Howard A. Stone and Ozgur Sahin, 7 June 2023, Nature. DOI: 10.1038/s41586-023-06144-y The study was funded by the U.S. Department of Energy, the Office of Naval Research, the National Institutes of Health, and the David and Lucile Packard Foundation. The illustration shows how different areas of PRC2 protein (the one on the right side) bind to survivin. The researchers chopped the PRC2 sequence into units of 15 amino acids and arranged them on a grid. Each pixel in that grid is 1 unit. The color shows binding strength to survivin. Blue means the unit in that pixel doesn’t bind/binds weakly to survivin, and the bright pink pixels are the strongest binders. Credit: Atsarina Larasati Anindya All living cells contain proteins with different functions, depending on the type of cell. Researchers have discovered a way to identify proteins even without looking at their structure. Their method is faster, easier, and more reliable than previous methods. Currently, the general view is that each protein’s structure is what controls its function in cells. The atomic sequences, meaning how the atoms are arranged in the proteins, create the protein’s structure and shape. But there are many proteins that lack a well-defined structure. Researcher Gergely Katona at the University of Gothenburg has developed a new method where proteins are scanned based on the number of amino acids (or the number of different atoms) they contain in order to identify them and their function instead of identifying them based on their structure. With this scanning method, the researchers were able to predict relatively reliably which combination of amino acids is needed to bind to the protein survivin. The outcome was a reliability of about 80 percent, which is better than when you use the protein’s primary structures for identification. The results are now published in the scientific journal iScience. Gergely Katona, Professor of Biochemistry at the University of Gothenburg. Credit: Torbjörn Nur Olsson The Structure of Less Importance Several thousand peptides containing 15 amino acids were tested and the researchers were able to conclude that it was the amino acid content that affected their binding to survivin, while the structure of the peptides had almost no significance. “Simple counting things has often been a successful method in science. Here we counted the number of amino acids and were able to predict the function of the protein surprisingly well,” says Gergely Katona. The researchers see advantages to this method of scanning proteins. Machine learning (AI) also speeds up the process of linking the number and type of amino acids to a certain function. This in turn means that the development of new biological drugs can be accelerated. In the researchers’ experiments with this new scanning method, a completely new function of the protein survivin was also discovered. This protein is mainly prominent in embryo cells and prevents programmed cell death. But in cancerous tumors, survivin becomes unregulated and thus facilitates the development of cancer. Useful in Cancer Research The researchers have now seen that survivin directly influences another protein, PRC2, which switches off and on various functions in the DNA in the cell, like a kind of programming. Dysfunctional PRC2 can also be linked to various forms of cancer. Today’s cancer drugs target both survivin and PRC2, but with the newly discovered link between survivin and PRC2, the drugs may need to be designed differently to avoid serious side effects. “We saw that if we suppressed the level of survivin, activity in PRC2 increased. The dream for pharmaceutical companies is to find the right targets in the atomic sequences to be able to balance the two proteins,” says Gergely Katona. Reference: “Survivin prevents the polycomb repressor complex 2 from methylating histone 3 lysine 27” by Maja Jensen, Venkataragavan Chandrasekaran, María-José García-Bonete, Shuxiang Li, Atsarina Larasati Anindya, Karin Andersson, Malin C. Erlandsson, Nina Y. Oparina, Björn M. Burmann, Ulrika Brath, Anna R. Panchenko, Maria Bokarewa I. and Gergely Katona, 29 May 2023, iScience. DOI: 10.1016/j.isci.2023.106976 RRG455KLJIEVEWWF |
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