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The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy

机译:通过Terahertz时域光谱研究单体和二聚体胰岛素的水合壳

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摘要

Protein aggregation is believed to be a significant biological mechanism related to neurodegenerative disease, which makes the early-stage detection of aggregates a major concern. We demonstrated the use of terahertz (THz) time-domain spectroscopy to study protein-water interaction of monomeric and dimeric bovine insulin in aqueous samples. Regulated by changing pH and verified by size-exclusion chromatography and dynamic light scattering, we then measured their concentration-dependent changes in THz absorption between 0.5 and 3.0 THz and quantitatively deduced the extended hydration shell thickness by cubic distribution model and random distribution model. Under a random distribution assumption, the extended hydration thickness is 15.4 +/- 0.4 angstrom for monomeric insulin and 17.5 +/- 0.5 angstrom for dimeric insulin, with the hydration number of 6700 and 11,000, respectively. The hydration number of dimeric insulin is not twice but 1.64 times that of monomeric insulin, further supported by the ratio of solvent-accessible surface area. This "1.64-times" relation probably originates from the structural and conformational changes accompanied with dimerization. Combined with the investigations on insulin samples with different single amino acid mutations, residue B24 is believed to play an important role in the dimerization process. It is demonstrated that THz time-domain spectroscopy is a useful tool and has the sensitivity to provide the hydration information of different protein aggregates at an early stage.
机译:据信蛋白质聚集是与神经变性疾病有关的显着生物机制,这使得党的早期检测成为主要问题。我们证明了使用Terahertz(THz)时域光谱学研究单体和二聚体牛胰岛素在水性样品中的蛋白水相互作用。通过改变pH调节并通过尺寸排阻色谱和动态光散射验证,然后通过立方分布模型和随机分布模型定量地,测量其浓度依赖性变化。在随机分布假设下,用于单体胰岛素的延伸水合厚度为15.4 +/- 0.4埃,二聚体胰岛素的17.5 +/- 0.5埃,分别为6700和11,000的水合次数。二聚体胰岛素的水合数不是单体胰岛素的两倍,但通过溶剂可接近的表面积的比例进一步支持。这个“1.64倍”关系可能来自结构和构象变化,伴随着二元化。结合不同单氨基酸突变的胰岛素样品的研究,认为残留物B24在二聚化过程中起重要作用。证明THz时域光谱是一种有用的工具,并且具有在早期阶段提供不同蛋白质聚集体的水化信息的敏感性。

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  • 来源
    《Biophysical Journal》 |2019年第3期|共9页
  • 作者单位

    Tianjin Univ Minist Educ China State Key Lab Precis Measuring Technol &

    Instrume Tianjin;

    Tianjin Univ Minist Educ China State Key Lab Chem Engn Tianjin Peoples R China;

    Tianjin Univ Minist Educ China Key Lab Optoelect Informat Technol Tianjin Peoples R China;

    Chinese Acad Sci Shanghai Inst Appl Phys Div Interfacial Water Shanghai Peoples R China;

    Tianjin Univ Minist Educ China State Key Lab Chem Engn Tianjin Peoples R China;

    Tianjin Univ Minist Educ China State Key Lab Precis Measuring Technol &

    Instrume Tianjin;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物物理学;
  • 关键词

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