瑞士洛桑联邦理工学院材料学院Francesco Stellacci研究组取得一项新突破。他们报道了氨基酸对蛋白质和胶体分散体的稳定作用。相关论文于2025年9月10日发表在《自然》杂志上。

在这里，研究团队推断AAs具有一种新的和广泛的胶体性质：它们通过弱相互作用吸附在纳米级胶体表面，从而稳定片状纳米胶体。研究组通过仔细的实验评估了AAs对各种蛋白质、质粒DNA和非生物纳米粒子分散体的稳定作用，证明了这一普遍特性。

此外，研究小组开发了一个理论框架来捕捉这一现象，并通过实验证实了几个新的广泛的理论含义，这些理论含义适用于AAs之外。体内实验进一步证明，添加1将脯氨酸转化为胰岛素，使其在血液中的生物利用度加倍。总的来说，他们的结果表明，小分子的作用是一样的。

据介绍，氨基酸（AAs）作为生物介质的稳定剂有着悠久的历史。例如，它们是生物医学制剂的重要组成部分。原子吸收剂对生物系统的影响也开始得到重视。例如，人们认为缺水的细胞会增加AAs的水平，从而阻止蛋白质聚集。关于它们的功能，人们提出了几种假设，从水结构到亲水性，再到防止错误折叠的稳定等特殊作用，但尚不清楚它们的稳定功能是蛋白质特有的还是一般的胶体性质。

附：英文原文

Title: Stabilizing effect of amino acids on protein and colloidal dispersions

Author: Mao, Ting, Xu, Xufeng, Winkler, Pamina M., Siri, Ccilia, Poliukhina, Ekaterina, Silva, Paulo Jacob, Xu, Nan, Hu, Yu, Al Zahabi, Karim, La Polla, Rmi, Luo, Zhi, Ong, Quy, Alexander-Katz, Alfredo, Stellacci, Francesco

Issue&Volume: 2025-09-10

Abstract: Amino acids (AAs) have a long history of being used as stabilizers for biological media1. For example, they are important components in biomedical formulations. The effect of AAs on biological systems is also starting to be appreciated. For example, it is believed that water-stressed cells increase the levels of AAs to prevent protein aggregation2. Several hypotheses have been put forward regarding their function, ranging from water-structuring3 to hydrotropic4 to specific effects such as stabilization against misfolding, yet it is not known whether their stabilizing function is protein specific or a generic colloidal property. Here we deduce that AAs possess a new and broad colloidal property: they stabilize patchy nanoscale colloids by adsorbing onto their surfaces through weak interactions. We demonstrate this general property by careful experimental evaluation of the stabilizing effect of AAs on dispersions of various proteins, plasmid DNA and non-biological nanoparticles. Furthermore, we develop a theoretical framework that captures this phenomenon and experimentally corroborate several new broad theoretical implications that apply beyond AAs. In vivo experiments further demonstrate that the addition of 1M proline to insulin doubles its bioavailability in blood. Overall, our results indicate that the role of small molecules is as

DOI: 10.1038/s41586-025-09506-w

Source: https://www.nature.com/articles/s41586-025-09506-w