دورية أكاديمية

Analysis of the effect of cations on protein conformational stability using solid-state nanopores.

التفاصيل البيبلوغرافية
العنوان: Analysis of the effect of cations on protein conformational stability using solid-state nanopores.
المؤلفون: Libo Zhu, Hongwen Wu, Zhengyuan Xu, Lanying Guo, Jinsong Zhao
المصدر: Analyst; 6/7/2024, Vol. 149 Issue 11, p3186-3194, 9p
مصطلحات موضوعية: PROTEIN stability, NANOPORES, PROTEIN conformation, DENATURATION of proteins, MONOVALENT cations
مستخلص: The conformation of proteins is closely related to their biological functions, and it is affected by many factors, including the type of cations in solution. However, it is difficult to detect the conformational changes of a protein in situ. As a single-molecule sensing technology, nanopores can convert molecular structural information into analyzable current signals within a reasonable time range. Herein, we detect and analyze the effects of two different types of monovalent cations (Na+ and Li+) on a model protein bovine serum albumin (BSA) conformation using SiNx nanopores with different diameters. The quantitative analysis results show that the excluded volume of BSA in LiCl salt solutions is larger than the value in NaCl solution, indicating that Li+ is more prone to unfolding the proteins and making them unstable. This study demonstrated that nanopores enable the in situ detection of the structure of proteins at the single-molecule level and provide a new approach for the quantitative analysis of proteins. [ABSTRACT FROM AUTHOR]
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قاعدة البيانات: Complementary Index
الوصف
تدمد:00032654
DOI:10.1039/d4an00248b