Suppr超能文献

酸性弹性蛋白样多肽的独特硅质仿生矿化,无需羟基和带电残基。

Unique silica biomimetic mineralization of acidic elastin-like polypeptides without hydroxyl and charged residues.

机构信息

Department of Bioengineering and Biotechnology, Huaqiao University, Xiamen 361021, Fujian, China.

Department of Bioengineering and Biotechnology, Huaqiao University, Xiamen 361021, Fujian, China.

出版信息

Int J Biol Macromol. 2020 Jun 15;153:224-231. doi: 10.1016/j.ijbiomac.2020.03.007. Epub 2020 Mar 3.

Abstract

Elastin-like polypeptides (ELPs), usually as a purification-tag, can be easily expressed and rapidly purified. We found ELPs[V9F-40], which did not contain hydroxyl or charged residues with the pI of 5.52, could biomimetically form silica when they were in ordered structure. The specific activity of ELPs[V9F-40] was 70.89 ± 9.53. Besides, the time needed for the completion of biomimetic silicification was about 138 s, which was only 1/3 of that for other reported peptides. The ELPs@silica is mainly spherical and the sizes of them were around 900 nm. However, currently presented mechanisms for peptide-triggered silica biomimetic mineralization could not explain such unique phenomenon. It would pave a new way for mining or designing peptides with such function, which provide a potential green method for the preparation of biomimetic silica particles. It would endow ELPs more functions and expand the application fields of ELPs such as the bioinspired synthesis of peptide biotemplated metal or nonmetal oxide nanoparticles.

摘要

弹性蛋白样多肽(ELPs)通常作为一种纯化标签,可以很容易地进行表达和快速纯化。我们发现,ELPs[V9F-40] 不含羟基或带有等电点为 5.52 的电荷残基,当它们处于有序结构时,可以仿生形成二氧化硅。ELPs[V9F-40] 的比活性为 70.89±9.53。此外,仿生硅化完成所需的时间约为 138 秒,仅为其他报道的肽所需时间的 1/3。ELPs@二氧化硅主要呈球形,直径约为 900nm。然而,目前报道的肽触发的二氧化硅仿生矿化机制无法解释这种独特的现象。这将为挖掘或设计具有这种功能的肽开辟新途径,为仿生二氧化硅颗粒的制备提供一种潜在的绿色方法。这将赋予 ELPs 更多的功能,并扩展 ELPs 的应用领域,如肽仿生合成金属或非金属氧化物纳米粒子。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验