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Temperature- and pH-dependent protein conformational changes investigated by terahertz dielectric spectroscopy

文献类型：期刊论文

作者Zang, Ziyi2,3,4; Yan, Shihan2,3; Hana, Xiaohui2,4; Wei, Dongshan1,3; Cui, Hong-Liang2,3,4; Du, Chunlei2
刊名INFRARED PHYSICS & TECHNOLOGY
出版日期2019-05-01
卷号98页码:260-265
关键词Terahertz dielectric spectroscopy Protein formulation Protein unfolding Temperature pH
ISSN号1350-4495
DOI10.1016/j.infrared.2019.03.021
通讯作者Cui, Hong-Liang(hcui@jlu.edu.cn)
英文摘要Polypeptides and protein drugs have received enormous attention from pharmaceutical industry, medical sector and consumer groups because of a favourable combination of their bioactivity, specificity and overall success rate for the treatment of a variety of diseases. The efficacy and safety of drugs may be degraded due to fluctuating environmental factors, accompanied by changes of the natural conformation of protein. Thus, it is necessary and meaningful to evaluate drug status before use. To that end, the evolving new and pre-existing protein activity/conformation technologies have proven to ensure the safety of drug use consistently. Recently, terahertz time-domain spectroscopy (THz-TDS) has demonstrated suitability for label-free and non-destructive detection of polypeptide and protein conformational changes. In this paper, THz optical parameters of pepsin solutions under different temperatures and with varying pH are measured to demonstrate the feasibility and the considerable potential of THz spectroscopic method in detecting protein drugs. In cases where temperature or pH change is apparent, the THz absorption coefficient, the refractive index, and the dielectric loss tangent change noticeably, independently verified by enzyme activity testing. These findings strongly support the conclusion that THz spectroscopy of pepsin solutions can be used for qualitative analysis to identify the folding or unfolding of protein drugs caused by changes of environmental factors, laying the foundation of a new label-free method for quality control of protein drugs.
资助项目National Key R&D Program of China[2016YFC0101301] ; National Key R&D Program of China[2017YFF0106303] ; National Key R&D Program of China[2016YFC0101002] ; National Natural Science Foundation of China[11504372] ; National Natural Science Foundation of China[61605206] ; National Natural Science Foundation of China[61771138]
WOS研究方向Instruments & Instrumentation ; Optics ; Physics
语种英语
WOS记录号WOS:000471361000032
出版者ELSEVIER SCIENCE BV
源URL[http://119.78.100.138/handle/2HOD01W0/8203]  
专题太赫兹技术研究中心
通讯作者Cui, Hong-Liang
作者单位1.Dongguan Univ Technol, Sch Elect Engn, Dongguan 523808, Guangdong, Peoples R China
2.Chinese Acad Sci, Chongqing Inst Green & Intelligent Technol, Chongqing Key Lab Multiscale Mfg Technol, Chongqing 400714, Peoples R China
3.Chinese Acad Sci, Chongqing Engn Res Ctr High Resolut & Three Dimen, Chongqing Inst Green & Intelligent Technol, Chongqing 400714, Peoples R China
4.Jilin Univ, Coll Instrumentat & Elect Engn, Changchun 130061, Jilin, Peoples R China
推荐引用方式
GB/T 7714		 Zang, Ziyi,Yan, Shihan,Hana, Xiaohui,et al. Temperature- and pH-dependent protein conformational changes investigated by terahertz dielectric spectroscopy[J]. INFRARED PHYSICS & TECHNOLOGY,2019,98:260-265.
APA Zang, Ziyi,Yan, Shihan,Hana, Xiaohui,Wei, Dongshan,Cui, Hong-Liang,&Du, Chunlei.(2019).Temperature- and pH-dependent protein conformational changes investigated by terahertz dielectric spectroscopy.INFRARED PHYSICS & TECHNOLOGY,98,260-265.
MLA Zang, Ziyi,et al."Temperature- and pH-dependent protein conformational changes investigated by terahertz dielectric spectroscopy".INFRARED PHYSICS & TECHNOLOGY 98(2019):260-265.

入库方式： OAI收割

来源：重庆绿色智能技术研究院

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