真空气相沉积法制备抗蛋白质低聚乙二醇自组装单硫醇层。

IF 2.1 4区 医学 Q2 Physics and Astronomy Biointerphases Pub Date : 2010-06-01 DOI:10.1116/1.3407483
Laxman Kankate, Udo Werner, Andrey Turchanin, Armin Gölzhäuser, Helge Grossmann, Robert Tampé
{"title":"真空气相沉积法制备抗蛋白质低聚乙二醇自组装单硫醇层。","authors":"Laxman Kankate,&nbsp;Udo Werner,&nbsp;Andrey Turchanin,&nbsp;Armin Gölzhäuser,&nbsp;Helge Grossmann,&nbsp;Robert Tampé","doi":"10.1116/1.3407483","DOIUrl":null,"url":null,"abstract":"<p><p>Protein resistant oligo(ethylene glycol) (OEG) terminated self-assembled monolayers (SAMs) of thiols on gold are commonly used for suppression of nonspecific protein adsorption in biology and biotechnology. The standard preparation for these SAMs is the solution method (SM) that involves immersion of the gold surface in an OEG solution. Here the authors present the preparation of 11-(mercaptoundecyl)-triethylene glycol [HS(CH(2))(11)(OCH(2)CH(2))(3)OH] SAMs on gold surface by vapor deposition (VD) in vacuum. They compare the properties of SAMs prepared by VD and SM using x-ray photoelectron spectroscopy (XPS), polarization modulation infrared reflection absorption spectroscopy, and surface plasmon resonance measurements. VD and SM SAMs exhibit similar packing density and show a similar resistance to the nonspecific adsorption of various proteins (bovine serum albumin, trypsin, and myoglobin) under physiological conditions. A very high sensitivity of the OEG SAMs to x-ray radiation is found, which allows tuning their protein resistance. These results show a new path to in situ engineering, analysis, and patterning of protein resistant OEG SAMs by high vacuum and ultrahigh vacuum techniques.</p>","PeriodicalId":49232,"journal":{"name":"Biointerphases","volume":null,"pages":null},"PeriodicalIF":2.1000,"publicationDate":"2010-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1116/1.3407483","citationCount":"20","resultStr":"{\"title\":\"Protein resistant oligo(ethylene glycol) terminated self-assembled monolayers of thiols on gold by vapor deposition in vacuum.\",\"authors\":\"Laxman Kankate,&nbsp;Udo Werner,&nbsp;Andrey Turchanin,&nbsp;Armin Gölzhäuser,&nbsp;Helge Grossmann,&nbsp;Robert Tampé\",\"doi\":\"10.1116/1.3407483\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Protein resistant oligo(ethylene glycol) (OEG) terminated self-assembled monolayers (SAMs) of thiols on gold are commonly used for suppression of nonspecific protein adsorption in biology and biotechnology. The standard preparation for these SAMs is the solution method (SM) that involves immersion of the gold surface in an OEG solution. Here the authors present the preparation of 11-(mercaptoundecyl)-triethylene glycol [HS(CH(2))(11)(OCH(2)CH(2))(3)OH] SAMs on gold surface by vapor deposition (VD) in vacuum. They compare the properties of SAMs prepared by VD and SM using x-ray photoelectron spectroscopy (XPS), polarization modulation infrared reflection absorption spectroscopy, and surface plasmon resonance measurements. VD and SM SAMs exhibit similar packing density and show a similar resistance to the nonspecific adsorption of various proteins (bovine serum albumin, trypsin, and myoglobin) under physiological conditions. A very high sensitivity of the OEG SAMs to x-ray radiation is found, which allows tuning their protein resistance. These results show a new path to in situ engineering, analysis, and patterning of protein resistant OEG SAMs by high vacuum and ultrahigh vacuum techniques.</p>\",\"PeriodicalId\":49232,\"journal\":{\"name\":\"Biointerphases\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.1000,\"publicationDate\":\"2010-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1116/1.3407483\",\"citationCount\":\"20\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biointerphases\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1116/1.3407483\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"Physics and Astronomy\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biointerphases","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1116/1.3407483","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Physics and Astronomy","Score":null,"Total":0}
引用次数: 20

摘要

在生物学和生物技术中,巯基硫醚的抗蛋白寡聚乙二醇(OEG)端自组装单层(SAMs)被广泛用于抑制非特异性蛋白质吸附。这些SAMs的标准制备方法是溶液法(SM),将金表面浸入OEG溶液中。本文采用真空气相沉积(VD)技术在金表面制备了11-(巯基癸基)-三甘醇[HS(CH(2))(11)(OCH(2)CH(2))(3)OH] SAMs。他们利用x射线光电子能谱(XPS)、偏振调制红外反射吸收光谱和表面等离子体共振测量比较了VD和SM制备的sam的性能。VD和SM SAMs具有相似的堆积密度,并且在生理条件下对各种蛋白质(牛血清白蛋白、胰蛋白酶和肌红蛋白)的非特异性吸附具有相似的抗性。发现OEG sam对x射线辐射具有非常高的灵敏度,这允许调整它们的蛋白质抗性。这些结果为利用高真空和超高真空技术进行耐蛋白OEG sam的原位工程、分析和图图化提供了新的途径。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Protein resistant oligo(ethylene glycol) terminated self-assembled monolayers of thiols on gold by vapor deposition in vacuum.

Protein resistant oligo(ethylene glycol) (OEG) terminated self-assembled monolayers (SAMs) of thiols on gold are commonly used for suppression of nonspecific protein adsorption in biology and biotechnology. The standard preparation for these SAMs is the solution method (SM) that involves immersion of the gold surface in an OEG solution. Here the authors present the preparation of 11-(mercaptoundecyl)-triethylene glycol [HS(CH(2))(11)(OCH(2)CH(2))(3)OH] SAMs on gold surface by vapor deposition (VD) in vacuum. They compare the properties of SAMs prepared by VD and SM using x-ray photoelectron spectroscopy (XPS), polarization modulation infrared reflection absorption spectroscopy, and surface plasmon resonance measurements. VD and SM SAMs exhibit similar packing density and show a similar resistance to the nonspecific adsorption of various proteins (bovine serum albumin, trypsin, and myoglobin) under physiological conditions. A very high sensitivity of the OEG SAMs to x-ray radiation is found, which allows tuning their protein resistance. These results show a new path to in situ engineering, analysis, and patterning of protein resistant OEG SAMs by high vacuum and ultrahigh vacuum techniques.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Biointerphases
Biointerphases BIOPHYSICS-MATERIALS SCIENCE, BIOMATERIALS
CiteScore
4.10
自引率
0.00%
发文量
35
审稿时长
>12 weeks
期刊介绍: Biointerphases emphasizes quantitative characterization of biomaterials and biological interfaces. As an interdisciplinary journal, a strong foundation of chemistry, physics, biology, engineering, theory, and/or modelling is incorporated into originated articles, reviews, and opinionated essays. In addition to regular submissions, the journal regularly features In Focus sections, targeted on specific topics and edited by experts in the field. Biointerphases is an international journal with excellence in scientific peer-review. Biointerphases is indexed in PubMed and the Science Citation Index (Clarivate Analytics). Accepted papers appear online immediately after proof processing and are uploaded to key citation sources daily. The journal is based on a mixed subscription and open-access model: Typically, authors can publish without any page charges but if the authors wish to publish open access, they can do so for a modest fee. Topics include: bio-surface modification nano-bio interface protein-surface interactions cell-surface interactions in vivo and in vitro systems biofilms / biofouling biosensors / biodiagnostics bio on a chip coatings interface spectroscopy biotribology / biorheology molecular recognition ambient diagnostic methods interface modelling adhesion phenomena.
期刊最新文献
Interleukin 1β and lipopolysaccharides induction dictate chondrocyte morphological properties and reduce cellular roughness and adhesion energy comparatively. Tutorial on the instrumentation of sum frequency generation vibrational spectroscopy: Using a Ti:sapphire based system as an example. Mass spectral imaging showing the plant growth-promoting rhizobacteria's effect on the Brachypodium awn. Time-of-flight secondary ion mass spectrometry analysis of hair samples using unsupervised artificial neural network. Ar-gas cluster ion beam in ToF-SIMS for peptide and protein analysis.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1