The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association

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	The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association
	Wei JC(韦佳辰); Dobnikar J; Curk T; Song F(宋凡)
刊名	PLOS ONE
	2016
通讯作者邮箱	songf@lnm.imech.ac.cn
卷号	11 期号:3 页码:e0151159
ISSN号	1932-6203
通讯作者	Song, F (reprint author), Chinese Acad Sci, Inst Mech, State Key Lab Nonlinear Mech LNM, Beijing 100190, Peoples R China.
产权排序	[Wei, Jiachen; Song, Fan] Chinese Acad Sci, Inst Mech, State Key Lab Nonlinear Mech LNM, Beijing 100190, Peoples R China; [Dobnikar, Jure] Beijing Univ Chem Technol, Int Res Ctr Soft Matter, Beijing 100029, Peoples R China; [Curk, Tine] Univ Cambridge, Univ Chem Lab, Lensfield Rd, Cambridge CB2 1EW, England
中文摘要	In living systems proteins are typically found in crowded environments where their effective interactions strongly depend on the surrounding medium. Yet, their association and dissociation needs to be robustly controlled in order to enable biological function. Uncontrolled protein aggregation often causes disease. For instance, cataract is caused by the clustering of lens proteins, i.e., crystallins, resulting in enhanced light scattering and impaired vision or blindness. To investigate the molecular origins of cataract formation and to design efficient treatments, a better understanding of crystallin association in macromolecular crowded environment is needed. Here we present a theoretical study of simple coarse grained colloidal models to characterize the general features of how the association equilibrium of proteins depends on the magnitude of intermolecular attraction. By comparing the analytic results to the available experimental data on the osmotic pressure in crystallin solutions, we identify the effective parameters regimes applicable to crystallins. Moreover, the combination of two models allows us to predict that the number of binding sites on crystallin is small, i.e. one to three per protein, which is different from previous estimates. We further observe that the crowding factor is sensitive to the size asymmetry between the reactants and crowding agents, the shape of the protein clusters, and to small variations of intermolecular attraction. Our work may provide general guidelines on how to steer the protein interactions in order to control their association.
分类号	二类
类目[WOS]	Multidisciplinary Sciences
研究领域[WOS]	Science & Technology - Other Topics
收录类别	SCI
原文出处	http://dx.doi.org/10.1371/journal.pone.0151159
语种	英语
WOS记录号	WOS:000371991300090
内容类型	期刊论文
源URL	[http://dspace.imech.ac.cn/handle/311007/59570]
专题	力学研究所_非线性力学国家重点实验室
推荐引用方式 GB/T 7714	Wei JC,Dobnikar J,Curk T,et al. The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association[J]. PLOS ONE,2016,11(3):e0151159.
APA	Wei JC,Dobnikar J,Curk T,&Song F.(2016).The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association.PLOS ONE,11(3),e0151159.
MLA	Wei JC,et al."The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association".PLOS ONE 11.3(2016):e0151159.