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

doi:10.1016/j.bpj.2019.06.028

CORC > 上海应用物理研究所 > 中国科学院上海应用物理研究所 > 中科院上海应用物理研究所2011-2017年

	The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy
	Wang, PF ; Wang, XC ; Liu, LY ; Zhao, HW ; Qi, W ; He, MX
刊名	BIOPHYSICAL JOURNAL
	2019
卷号	117 期号:3 页码:533-541
关键词	WATER DYNAMICS PROTEIN AGGREGATION DISSOCIATION FIBRILS MOLECULES DIFFUSION RESONANCE BINDING NMR
ISSN号	0006-3495
DOI	10.1016/j.bpj.2019.06.028
文献子类	期刊论文
英文摘要	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.
语种	英语
内容类型	期刊论文
源URL	[http://ir.sinap.ac.cn/handle/331007/32246]
专题	上海应用物理研究所_中科院上海应用物理研究所2011-2017年
作者单位	1.Chinese Acad Sci, Shanghai Inst Appl Phys, Key Lab Interfacial Phys & Technol, Shanghai, Peoples R China 2.Tianjin Univ, Minist Educ China, Key Lab Optoelect Informat Technol, Tianjin, Peoples R China; 3.Chinese Acad Sci, Shanghai Inst Appl Phys, Div Interfacial Water, Shanghai, Peoples R China; 4.Tianjin Univ, Minist Educ China, State Key Lab Precis Measuring Technol & Instrume, Tianjin, Peoples R China; 5.Tianjin Univ, Minist Educ China, State Key Lab Chem Engn, Tianjin, Peoples R China;
推荐引用方式 GB/T 7714	Wang, PF,Wang, XC,Liu, LY,et al. The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy[J]. BIOPHYSICAL JOURNAL,2019,117(3):533-541.
APA	Wang, PF,Wang, XC,Liu, LY,Zhao, HW,Qi, W,&He, MX.(2019).The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy.BIOPHYSICAL JOURNAL,117(3),533-541.
MLA	Wang, PF,et al."The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy".BIOPHYSICAL JOURNAL 117.3(2019):533-541.