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首页> 外文期刊>Langmuir: The ACS Journal of Surfaces and Colloids >Sequential Adsorption of Bovine Mucin and Lactoperoxidase to Various Substrates Studied with Quartz Crystal Microbalance with Dissipation
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Sequential Adsorption of Bovine Mucin and Lactoperoxidase to Various Substrates Studied with Quartz Crystal Microbalance with Dissipation

机译:耗散的石英晶体微天平研究牛黏蛋白和乳过氧化物酶对各种基质的连续吸附

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摘要

Mucin and lactoperoxidase are both natively present in the human saliva. Mucin provides lubricating and antiadhesive function, while lactoperoxidase has antimicrobial activity. We propose that combined Films of the two proteins can be used as a strategy for surface modification in biomedical applications such as implants or biosensors. In order to design and ultilize mixed protein films, it is necessary to understand the variation in adsorption behavior of the proteins onto different surfaces and how it affects their interaction. The quartz crystal microbalance with dissipation (QCM-D) technique hats been used to extract information of the adsorption properties of bovine mucin (BSM) and lactoperoxidase (LPO) to gold, silica. and hydrophobized silica surfaces. The information has further been used to retrieve information of the viscoelastic properties of the adsorbed film. The adsorption and compaction of BSM were found to vary depending on the nature of the underlying bare surface, adsorbing as at thick highly hydrated film with loops and tails extending out in the bulk on gold and as a thinner film with much lower adsorbed amount on silica; and on hydrophobic surfaces, BSM adsorbs as a flat and much more compact layer. On gold and silica, the highly hydrated BSM film is cross-linked and compacted by the addition of LPO, whereas the compaction is not as pronounced on the already more compact film formed on hydrophobic surfaces. The adsorption of LPO to bare surfaces also varied depending on the type of surface. The adsorption profile of BSM onto LPO-coated surfaces mimicked the adsorption to the underlying surface, implying little interaction between the LPO and BSM. The interaction between the protein layers was interpreted as a combination of electrostatic and hydrophobic interactions, which was in turn influenced by the interaction of the proteins with the different substrates.
机译:粘蛋白和乳过氧化物酶都天然存在于人类唾液中。粘蛋白提供润滑和抗粘连功能,而乳过氧化物酶则具有抗菌活性。我们建议两种蛋白质的组合膜可以用作生物医学应用(例如植入物或生物传感器)中表面修饰的策略。为了设计和利用混合的蛋白质薄膜,有必要了解蛋白质在不同表面上的吸附行为的变化及其对蛋白质相互作用的影响。带有耗散的石英微天平(QCM-D)技术用于提取牛粘蛋白(BSM)和乳过氧化物酶(LPO)对金,二氧化硅的吸附性能信息。和疏水的二氧化硅表面。该信息还被用于获取吸附膜的粘弹性质的信息。发现BSM的吸附和压实度随下面裸露表面的性质而变化,在厚厚的高度水合的膜上吸附,其环和尾部在金块中向外延伸,而在较薄的膜上,二氧化硅的吸附量低得多;在疏水性表面上,BSM吸附为平坦且致密的层。在金和二氧化硅上,高度水合的BSM膜通过添加LPO交联并压实,而在疏水性表面上已经形成的更加致密的膜上,压实效果不那么明显。 LPO在裸露表面上的吸附也随表面类型而变化。 BSM在LPO涂层表面上的吸附曲线模拟了对下层表面的吸附,这意味着LPO与BSM之间几乎没有相互作用。蛋白质层之间的相互作用被解释为静电和疏水相互作用的组合,而静电和疏水相互作用又受蛋白质与不同底物相互作用的影响。

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