Biomimetic supported lipid bilayers with high cholesterol content formed by α-helical peptide-induced vesicle fusion.

Gregory J Hardy, Rahul Nayak, S Munir Alam, Joseph G Shapter, Frank Heinrich, Stefan Zauscher
{"title":"Biomimetic supported lipid bilayers with high cholesterol content formed by α-helical peptide-induced vesicle fusion.","authors":"Gregory J Hardy, Rahul Nayak, S Munir Alam, Joseph G Shapter, Frank Heinrich, Stefan Zauscher","doi":"10.1039/C2JM32016A","DOIUrl":null,"url":null,"abstract":"<p><p>In this study, we present a technique to create a complex, high cholesterol-containing supported lipid bilayers (SLBs) using α-helical (AH) peptide-induced vesicle fusion. Vesicles consisting of POPC : POPE : POPS : SM : Chol (9.35 : 19.25 : 8.25 : 18.15 : 45.00) were used to form a SLB that models the native composition of the human immunodeficiency virus-1 (HIV-1) lipid envelope. In the absence of AH peptides, these biomimetic vesicles fail to form a complete SLB. We verified and characterized AH peptide-induced vesicle fusion by quartz crystal microbalance with dissipation monitoring, neutron reflectivity, and atomic force microscopy. Successful SLB formation entailed a characteristic frequency shift of -35.4 ± 2.0 Hz and a change in dissipation energy of 1.91 ± 0.52 × 10<sup>-6</sup>. Neutron reflectivity measurements determined the SLB thickness to be 49.9 <sup>+1.9</sup><sub>-1.5</sub> Å, and showed the SLB to be 100 <sup>+0.0</sup><sub>-0.1</sub>% complete and void of residual AH peptide after washing. Atomic force microscopy imaging confirmed complete SLB formation and revealed three distinct domains with no visible defects. This vesicle fusion technique gives researchers access to a complex SLB composition with high cholesterol content and thus the ability to better recapitulate the native HIV-1 lipid membrane.</p>","PeriodicalId":16297,"journal":{"name":"Journal of Materials Chemistry","volume":"22 37","pages":"19506-19513"},"PeriodicalIF":0.0000,"publicationDate":"2012-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728912/pdf/nihms-389673.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Materials Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1039/C2JM32016A","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

In this study, we present a technique to create a complex, high cholesterol-containing supported lipid bilayers (SLBs) using α-helical (AH) peptide-induced vesicle fusion. Vesicles consisting of POPC : POPE : POPS : SM : Chol (9.35 : 19.25 : 8.25 : 18.15 : 45.00) were used to form a SLB that models the native composition of the human immunodeficiency virus-1 (HIV-1) lipid envelope. In the absence of AH peptides, these biomimetic vesicles fail to form a complete SLB. We verified and characterized AH peptide-induced vesicle fusion by quartz crystal microbalance with dissipation monitoring, neutron reflectivity, and atomic force microscopy. Successful SLB formation entailed a characteristic frequency shift of -35.4 ± 2.0 Hz and a change in dissipation energy of 1.91 ± 0.52 × 10-6. Neutron reflectivity measurements determined the SLB thickness to be 49.9 +1.9-1.5 Å, and showed the SLB to be 100 +0.0-0.1% complete and void of residual AH peptide after washing. Atomic force microscopy imaging confirmed complete SLB formation and revealed three distinct domains with no visible defects. This vesicle fusion technique gives researchers access to a complex SLB composition with high cholesterol content and thus the ability to better recapitulate the native HIV-1 lipid membrane.

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
α螺旋肽诱导囊泡融合形成的高胆固醇含量仿生支撑脂质双分子层。
在本研究中,我们介绍了一种利用α-螺旋(AH)肽诱导的囊泡融合技术来创建复杂的高胆固醇支撑脂质双分子层(SLB)的技术。由 POPC : POPE : POPS : SM : Chol (9.35 : 19.25 : 8.25 : 18.15 : 45.00) 组成的囊泡被用来形成模拟人类免疫缺陷病毒-1(HIV-1)脂质包膜原生成分的支撑脂质双层膜(SLB)。在缺乏 AH 肽的情况下,这些仿生囊泡无法形成完整的 SLB。我们通过石英晶体微天平耗散监测、中子反射和原子力显微镜验证并鉴定了AH肽诱导的囊泡融合。SLB的成功形成需要-35.4 ± 2.0 Hz的特征频率偏移和1.91 ± 0.52 × 10-6的耗散能量变化。中子反射率测量确定 SLB 厚度为 49.9 +1.9-1.5 Å,并显示 SLB 的完整度为 100 +0.0-0.1%,且在清洗后没有残留的 AH 肽。原子力显微镜成像证实了 SLB 的完整形成,并显示出三个不同的畴,没有明显的缺陷。这种囊泡融合技术使研究人员能够获得高胆固醇含量的复杂SLB成分,从而能够更好地再现原生HIV-1脂膜。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Journal of Materials Chemistry
Journal of Materials Chemistry 工程技术-材料科学:综合
自引率
0.00%
发文量
0
审稿时长
1.5 months
期刊最新文献
Improved anti-proliferative effect of doxorubicin-containing polymer nanoparticles upon surface modification with cationic groups. Anisotropic nanocrystal arrays organized on protein lattices formed by recombinant clathrin fragments. The effect of mineral coating morphology on mesenchymal stem cell attachment and expansion. Location-tuned relaxivity in Gd-doped mesoporous silica nanoparticles. Photoreactive elastin-like proteins for use as versatile bioactive materials and surface coatings.
×
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