返回资讯中心
外部精选
芯片&算力
#评测#基础设施#AI#Science#Biology#catalysts

Researchers use AI to design proteins that cut up other proteins

AI design tools make proteins that break bonds that are stable for hundreds of years.

Ars Technica John Timmer 2026/10/14 · 12 天前4 分钟阅读

以下正文同步自 Ars Technica,版权归原站所有,已转换为易读排版。

A protein is a chain of amino acids held together by what are called peptide bonds. On their own, those bonds are extremely stable; they're estimated to have a half-life of several hundred years. But in Earth's environment, most proteins don't last nearly that long. That's because organisms have evolved a handful of ways to catalyze the break-up of peptide bonds, which have diversified into countless specialized protein-digesting enzymes. Proteases are everywhere and generally make short work of any proteins that find their way into the environment. Now, researchers have basically short-circuited the diversification process, using AI-based protein design tools to take the catalytic core of two types of protease and replace the entire rest of the protein. The resulting enzymes could be tuned to cut specific proteins in half, and the researchers demonstrated their effectiveness by using them to cut proteins associated with neurological diseases. Cutting proteins The basic peptide bond isn't especially interesting-looking—it's what you get when you link an amino group to an acid, releasing a water molecule in the process. As their name implies, amino acids have both an amino and an acid group, allowing them to form peptide bonds on two sides of the amino acid. This is critical for building up the long chains found in proteins. (The amino acids also have side chains with distinctive chemistry, which gives a backbone specific properties.) Read full article Comments

正文由 探How 从来源站点 RSS 同步,内容未经改写;遇到排版缺失或需要图片、视频时请以原文为准。

打开原文
去社区讨论 →