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利用金属有机框架纳米孔选择性去除变性蛋白质

Selective Removal of Denatured Proteins Using MOF Nanopores.

作者信息

Taketomi Hirotaka, Hosono Nobuhiko, Uemura Takashi

机构信息

Department of Applied Chemistry, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, 113-8656 Tokyo, Japan.

出版信息

J Am Chem Soc. 2024 Jun 6. doi: 10.1021/jacs.4c03886.

Abstract

Here we present, for the first time, the selective adsorption of denatured proteins using a metal-organic framework (MOF), demonstrating promising potential for protein purification. Typical proteins, such as lysozyme and carbonic anhydrase B, enter the pores of MIL-101 through their narrow apertures when they are denatured to an unfolded state. Selective adsorption is achieved by finely tuning two key features: the sizes of the aperture and cage of the MOF nanopores, which are responsible for sorting unfolded polypeptide chains and inhibiting the translocation of the native form into the pores, respectively. By leveraging this selective adsorption, we successfully purified a mixture of native and denatured proteins by adding MOF to the mixture, achieving a native purity of over 99%.

摘要

在此,我们首次展示了使用金属有机框架(MOF)对变性蛋白质进行选择性吸附,这显示出在蛋白质纯化方面的巨大潜力。典型的蛋白质,如溶菌酶和碳酸酐酶B,在变性至未折叠状态时会通过其狭窄的孔径进入MIL-101的孔中。通过精细调节两个关键特性实现选择性吸附:MOF纳米孔的孔径和笼的尺寸,它们分别负责对未折叠的多肽链进行分选并抑制天然形式的蛋白质进入孔中。通过利用这种选择性吸附,我们通过向混合物中添加MOF成功纯化了天然和变性蛋白质的混合物,实现了超过99%的天然纯度。

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