• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

纤维蛋白原在模型聚合物上的吸附及构象变化:分子间重排的新方面

Fibrinogen adsorption and conformational change on model polymers: novel aspects of mutual molecular rearrangement.

作者信息

Berglin Mattias, Pinori Emiliano, Sellborn Anders, Andersson Marcus, Hulander Mats, Elwing Hans

机构信息

Department of Cell and Molecular Biology, Interface Biophysics, Göteborg University, and Department of Surgery, Sahlgrenska University Hospital, Göteborg SE-40530, Sweden.

出版信息

Langmuir. 2009 May 19;25(10):5602-8. doi: 10.1021/la803686m.

DOI:10.1021/la803686m
PMID:19366199
Abstract

By combining quartz crystal microbalance with dissipation monitoring (QCM-D) and surface plasmon resonance (SPR), the organic mass, water content, and corresponding protein film structure of fibrinogen adsorbed to acrylic polymeric substrates with varying polymer chain flexibility was investigated. Albumin and immunoglobulin G were included as reference proteins. For fibrinogen, the QCM-D model resulted in decreased adsorbed mass with increased polymer chain flexibility. This stands in contrast to the SPR model, in which the adsorbed mass increased with increased polymer chain flexibility. As the QCM-D model includes the hydrodynamically coupled water, we propose that on the nonflexible polymer significant protein conformational change with water incorporation in the protein film takes place. Fibrinogen maintained a more native conformation on the flexible polymer, probably due to polymer chain rearrangement rather than protein conformational change. In comparison with immunoglobulin G and albumin, polymer chain flexibility had only minor impact on adsorbed mass and protein structure. Understanding the adsorption and corresponding conformational change of a protein together with the mutual rearrangement of the polymer chain upon adsorption not only has implications in biomaterial science but could also increase the efficacy of molecular imprinted polymers (MIPs).

摘要

通过结合石英晶体微天平与耗散监测(QCM-D)以及表面等离子体共振(SPR),研究了吸附在具有不同聚合物链柔性的丙烯酸类聚合物基底上的纤维蛋白原的有机质量、含水量及相应的蛋白质膜结构。白蛋白和免疫球蛋白G作为参考蛋白质。对于纤维蛋白原,QCM-D模型显示随着聚合物链柔性增加,吸附质量降低。这与SPR模型相反,在SPR模型中吸附质量随聚合物链柔性增加而增加。由于QCM-D模型包含流体动力学耦合水,我们提出在刚性聚合物上,蛋白质膜中随着水的掺入发生了显著的蛋白质构象变化。纤维蛋白原在柔性聚合物上保持更天然的构象,这可能是由于聚合物链重排而非蛋白质构象变化。与免疫球蛋白G和白蛋白相比,聚合物链柔性对吸附质量和蛋白质结构的影响较小。了解蛋白质的吸附及相应的构象变化以及吸附时聚合物链的相互重排不仅对生物材料科学有意义,还可能提高分子印迹聚合物(MIP)的功效。

相似文献

1
Fibrinogen adsorption and conformational change on model polymers: novel aspects of mutual molecular rearrangement.纤维蛋白原在模型聚合物上的吸附及构象变化:分子间重排的新方面
Langmuir. 2009 May 19;25(10):5602-8. doi: 10.1021/la803686m.
2
Formation of viscoelastic protein layers on polymeric surfaces relevant to platelet adhesion.与血小板黏附相关的聚合物表面上黏弹性蛋白层的形成。
J Biomed Mater Res A. 2005 Mar 15;72(4):420-7. doi: 10.1002/jbm.a.30272.
3
Protein-associated water and secondary structure effect removal of blood proteins from metallic substrates.从金属基底上去除与蛋白质结合的水和二级结构效应的血蛋白质。
Langmuir. 2011 Mar 1;27(5):1830-6. doi: 10.1021/la1041794. Epub 2010 Dec 23.
4
Viscoelastic properties of fibrinogen adsorbed to the surface of biomaterials used in blood-contacting medical devices.吸附于血液接触医疗设备中所使用生物材料表面的纤维蛋白原的粘弹性特性。
Langmuir. 2007 Mar 13;23(6):3298-304. doi: 10.1021/la060500r. Epub 2007 Feb 10.
5
Fabrication of hydroxyapatite ultra-thin layer on gold surface and its application for quartz crystal microbalance technique.金表面羟基磷灰石超薄层的制备及其在石英晶体微天平技术中的应用。
Biomaterials. 2006 Nov;27(33):5748-54. doi: 10.1016/j.biomaterials.2006.07.029. Epub 2006 Aug 14.
6
Simultaneous surface plasmon resonance and quartz crystal microbalance with dissipation monitoring measurements of biomolecular adsorption events involving structural transformations and variations in coupled water.同时进行表面等离子体共振和石英晶体微天平测量,并监测涉及结构转变和耦合水变化的生物分子吸附事件中的耗散情况。
Anal Chem. 2004 Dec 15;76(24):7211-20. doi: 10.1021/ac0492970.
7
Analysis of interpenetrating polymer networks via quartz crystal microbalance with dissipation monitoring.通过带耗散监测的石英晶体微天平对互穿聚合物网络进行分析。
Langmuir. 2005 Jun 7;21(12):5529-36. doi: 10.1021/la0470737.
8
125I-radiolabeling, surface plasmon resonance, and quartz crystal microbalance with dissipation: three tools to compare protein adsorption on surfaces of different wettability.125I放射性标记、表面等离子体共振和带耗散的石英晶体微天平:用于比较蛋白质在不同润湿性表面上吸附情况的三种工具。
Langmuir. 2014 Feb 4;30(4):1029-35. doi: 10.1021/la403498w. Epub 2014 Jan 21.
9
Fibronectin and bovine serum albumin adsorption and conformational dynamics on inherently conducting polymers: a QCM-D study.纤维连接蛋白和牛血清白蛋白在本征导电聚合物上的吸附和构象动力学:QCM-D 研究。
Langmuir. 2012 Jun 5;28(22):8433-45. doi: 10.1021/la300692y. Epub 2012 May 22.
10
Conformational changes of fibrinogen after adsorption.吸附后纤维蛋白原的构象变化
J Phys Chem B. 2005 Nov 24;109(46):22027-35. doi: 10.1021/jp054456k.

引用本文的文献

1
Utilisation of Quartz Crystal Microbalance Sensors with Dissipation (QCM-D) for a Clauss Fibrinogen Assay in Comparison with Common Coagulation Reference Methods.与常用凝血参考方法相比,使用带耗散功能的石英晶体微天平传感器(QCM-D)进行克劳斯纤维蛋白原测定
Sensors (Basel). 2016 Feb 24;16(3):282. doi: 10.3390/s16030282.
2
Proteins, platelets, and blood coagulation at biomaterial interfaces.生物材料界面处的蛋白质、血小板与血液凝固
Colloids Surf B Biointerfaces. 2014 Dec 1;124:49-68. doi: 10.1016/j.colsurfb.2014.09.040. Epub 2014 Sep 28.
3
Mechanistic understanding of protein-silicone oil interactions.
蛋白质-硅油相互作用的机制理解。
Pharm Res. 2012 Jun;29(6):1689-97. doi: 10.1007/s11095-012-0696-6. Epub 2012 Feb 14.
4
Sensing surface PEGylation with microcantilevers.微悬臂梁的传感表面聚乙二醇化。
Beilstein J Nanotechnol. 2010;1:3-13. doi: 10.3762/bjnano.1.2. Epub 2010 Nov 22.
5
Innate immunity activation on biomaterial surfaces: a mechanistic model and coping strategies.生物材料表面固有免疫激活:一种机制模型与应对策略。
Adv Drug Deliv Rev. 2011 Sep 16;63(12):1042-50. doi: 10.1016/j.addr.2011.06.012. Epub 2011 Jul 8.