Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability

doi:10.1126/sciadv.abb7620

	Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability
	Ou, Xinwen 1; Xue, Bin 2; Lao, Yichong 1; Wutthinitikornkit, Yanee 1; Tian, Ranran 1; Zou, Aodong 1; Yang, Lingyun3 ; Wang, Wei 2; Cao, Yi 2; Li, Jingyuan 1
	2020-09
发表期刊	SCIENCE ADVANCES
ISSN	2375-2548
卷号	6 期号:39
DOI	10.1126/sciadv.abb7620
摘要	Mussels can strongly adhere to hydrophilic minerals in sea habitats by secreting adhesive proteins. The adhesion ability of these proteins is often attributed to the presence of Dopa derived from posttranslational modification of Tyr, whereas the contribution of structural feature is overlooked. It remains largely unknown how adhesive proteins overcome the surface-bound water layer to establish underwater adhesion. Here, we use molecular dynamics simulations to probe the conformations of adhesive protein Pvfp-5. and its salt-tolerant underwater adhesion on superhydrophilic mica. Dopa and positively charged basic residues form pairs, in this intrinsically disordered protein, and these residue pairs can lead to firm surface binding. Our simulations further suggest that the unmodified Tyr shows similar functions on surface adhesion by forming pairing structure with a positively charged residue. We confirm the presence of these residue pairs and verify the strong binding ability of unmodified proteins using nuclear magnetic resonance spectroscopy and lap shear tests.
收录类别	SCI ; SCIE ; EI
语种	英语
资助项目	National Natural Science Foundation of China[11722434][11874319][11674153][11804148][21904088] ; China Postdoctoral Science Foundation[2018M642401][2019T120499] ; National Natural Science Foundation of Jiangsu Province[BK20180320]
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000575531700028
出版者	AMER ASSOC ADVANCEMENT SCIENCE
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/123589
专题	iHuman研究所_公共科研平台_生命科学NMR平台
通讯作者	Cao, Yi; Li, Jingyuan
作者单位	1.Zhejiang Univ, Dept Phys, Zhejiang Prov Key Lab Quantum Technol & Device, Inst Quantitat Biol, Zheda Rd 38, Hangzhou 310027, Peoples R China; 2.Nanjing Univ, Dept Phys, Natl Lab Solid State Microstruct, Collaborat Innovat Ctr Adv Microstruct, Nanjing 210093, Peoples R China; 3.Shanghai Tech Univ, iHuman Inst, 393 Hua Xia Zhong Rd, Shanghai 201210, Peoples R China
推荐引用方式 GB/T 7714	Ou, Xinwen,Xue, Bin,Lao, Yichong,et al. Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability[J]. SCIENCE ADVANCES,2020,6(39).
APA	Ou, Xinwen.,Xue, Bin.,Lao, Yichong.,Wutthinitikornkit, Yanee.,Tian, Ranran.,...&Li, Jingyuan.(2020).Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability.SCIENCE ADVANCES,6(39).
MLA	Ou, Xinwen,et al."Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability".SCIENCE ADVANCES 6.39(2020).