A mussel polyphenol oxidase-like protein shows thiol-mediated antioxidant activity
A mussel polyphenol oxidase-like protein shows thiol-mediated antioxidant activity
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贻贝多酚氧化酶样蛋白显示硫醇介导的抗氧化活性
DOI：
10.1016/j.eurpolymj.2019.01.069
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发表时间：
2019
影响因子：
6
通讯作者：
T. Scheibel
中科院分区：
文献类型：
--
作者：
Jia Wang;Michael H. Suhre;T. Scheibel
海洋贻贝利用带有翻译后修饰氨基酸（如3,4-二羟基苯丙氨酸（DOPA）残基）的粘附蛋白在水下粘附在各种底物上，这是一个关键的化学特征。DOPA在海水中容易自动氧化，降低了附着强度，但有助于底层蛋白质的后续内聚（交联）。为了保持还原和氧化形式的DOPA具有相应的粘附和内聚性能，贻贝的水下粘附需要严格的氧化还原调节。本研究利用不同的退化PCR引物对贻贝足cDNA文库进行筛选，鉴定了贻贝足的全长多酚氧化酶样蛋白（PPOL）。在大肠杆菌中成功制备了重组PPOL （rPPOL）。rppo表现出巯基依赖性抗氧化活性，抑制DOPA氧化。这一发现为DOPA化学如何调节提供了见解，并可能激发DOPA介导的粘附材料的未来应用。
Marine mussels adhere underwater to a variety of substrates using adhesive proteins with post-translationally modified amino acids, such as 3,4-dihydroxyphenylalanine (DOPA) residues, as a key chemical signature. DOPA can auto-oxidize easily in seawater reducing the adhesion strength, but contributing to subsequent cohesion (cross-linking) of the underlying proteins. To maintain both reduced and oxidized forms of DOPA with corresponding adhesion and cohesion properties, strict redox regulation is necessary for mussel underwater adhesion. In this study, a full-length polyphenol oxidase-like protein (PPOL) fromMytilus galloprovincialiswas identified after screening of a mussel foot cDNA library using different degenerated PCR primers. The recombinant PPOL (rPPOL) was successfully produced inEscherichia coli. The rPPOL exhibits thiol-dependent antioxidant activity suppressing DOPA oxidation. This finding provides insights into how DOPA chemistry could be regulated and presumably inspires future applications of DOPA-mediated adhesion materials.
影响因子：
3
作者：
Winther, Jakob R.;Thorpe, Colin
通讯作者：
Thorpe, Colin
影响因子：
2.9
作者：
Nicklisch SC;Spahn JE;Zhou H;Gruian CM;Waite JH
通讯作者：
Waite JH
影响因子：
9.7
作者：
Wei, Wei;Tan, Yerpeng;Rodriguez, Nadine R. Martinez;Yu, Jing;Israelachvili, Jacob N.;Waite, J. Herbert
通讯作者：
Waite, J. Herbert