久热久草在线_一一高清视频在线观看_在线观看91av_久草免费在线观看视频_国产精品午夜无码A体验区_国产一级高清

English | 中文版 | 手機版 企業登錄 | 個人登錄 | 郵件訂閱
當前位置 > 首頁 > 技術文章 > 類天然環境中膜蛋白的熒光成像

類天然環境中膜蛋白的熒光成像

瀏覽次數:369 發布日期:2024-11-18  來源:本站 僅供參考,謝絕轉載,否則責任自負
Paper of the Month - #SMALPS
 
Your literary summer snack for September is here. Join us as we dive into the exciting realms of in vitro fluorescence studies of membrane proteins. Known to be a very challenging field, but new techniques are emerging.
The research was conducted in the Imperiali Lab, situated at the MIT, by Jean-Marie Swiecicki, Jordan Tyler Santana, and the namesake Barbara Imperiali, who are members of the departments of biology, physics and chemistry.
The challenging nature of membrane proteins
Membrane proteins are ubiquitous and play a crucial role in the cellular processes of all living systems (Fig. 1). They are the first point of interaction between cells and their surroundings since they are located at the cell's edge. As such, they mediate how cells sense and engage with their environment, converse with one another, and strictly regulate what enters and exits the cell. Not surprisingly, they are also the linchpin of the pharmaceutical industry. Although they represent about a third of the known human protein-coding genes, they are targeted by roughly 60% of the currently approved drugs. Unfortunately, at par with their biomedical value is the difficulty of characterizing them.

Their study proves to be challenging due to their hydrophobic nature and sensitivity to surrounding native environments. So far, traditional detergent-based methods often involved the detachment of these proteins from their native environment, which can alter their structure and function, and which is a time-consuming process. To address this issue, Swiecicki, Santana, and Imperiali introduce a strategic technique for fluorescence imaging that allows the visualization of membrane proteins while maintaining their native-like environment.
 
 
 
Fig. 1: Membrane proteins inside the cell membrane. Only this native environment ensures completely that the membrane proteins are folded correctly and thus are functional. Hydrophobic surface areas of the proteins are located inside the membrane while hydrophilic surfaces are located outside in either the ECM or cytosol.
 
Shine a light into native membrane environments
Their main strategy involved using a combination of genetically encoded non-canonical amino acids (ncAAs), bioorthogonal labeling, and detergent-free membrane protein solubilization based on an amphiphilic styrene-maleic acid polymer. Or in short: SMA. The researchers genetically incorporated ncAAs into the target membrane protein (Fig. 2).
 
Technical Dive
By repurposing a non-sense codon, most frequently the amber stop codon (TAG), ncAAs can be introduced. The inclusion of a generated tRNA synthetase/tRNATAG pair is necessary for this extension of the genetic code, known as amber suppression. As the fluorescent properties of ncAAs aren’t sufficient for single-molecule imaging applications, bioorthogonal labeling with a fluorescent dye compatible with single-molecule studies can help here.
 
These ncAAs contain specific chemical handles that can react selectively with fluorescent tags. By introducing these tags, which are compatible with living cells, they can achieve site-specific labeling of the protein within the cell membrane. All combined, this enables impressive single-molecule fluorescence studies.
 
 
Fig. 2: Explanation on how Swiecicki's approach for Single-molecule imaging worked.
1. Detergent free solubilization & stabilization of the membrane protein inside the SMALP (SMA-Lipid-Particle / Nanodisc).
2. Membrane proteins have the unnatural amino acid Bicyclononyne incorporated that carries specific chemical handles that can react selectively with fluorescent tags.
3. Due to there only being one membrane protein molecule per nanodisc each signal is ensured to come only from one molecule.
In their paper Swiecicki, Santana, and Imperiali emphasize the importance of preserving native-like environments of membrane proteins to create profound research conditions. Hence, their approach aims to minimize the disruption to the protein's structure and function, enabling them to observe its behavior in a more realistic setting.

In summary, the paper introduces a strategic method for fluorescence imaging of membrane proteins within their native-like environment. This approach involves genetically incorporating unnatural amino acids with specific chemical handles, allowing for site-specific labeling of the protein using fluorescent probes.
This innovation has the potential to revolutionize the study of membrane proteins by enabling more accurate observations of their behavior and interactions within living cells. It might also result in a greater comprehension of their biological roles and the possible therapeutic applications that result from these discoveries.
Sources
· Swiecicki JM, Santana JT, Imperiali B. A Strategic Approach for Fluorescence Imaging of Membrane Proteins in a Native-like Environment. Cell Chem Biol. 2020;27(2):245-251.e3. doi:10.1016/j.chembiol.2019.11.008
Keywords: Unnatural amino acids, Bioorthogonal labeling, SMA copolymers, Membrane proteins, Fluorescence studies
 
發布者:正民德思生物科技有限公司
聯系電話:028-85568133
E-mail:marketing@zenmindes.com

用戶名: 密碼: 匿名 快速注冊 忘記密碼
評論只代表網友觀點,不代表本站觀點。 請輸入驗證碼: 8795
Copyright(C) 1998-2025 生物器材網 電話:021-64166852;13621656896 E-mail:info@bio-equip.com
主站蜘蛛池模板: 国产毛片精品一区二区 | 在线免费看黄色 | 中国精品一区二区三区 | 国产欧美日韩高清在线不卡 | 久久黄色一级片 | 精品免费国产一区二区三区 | 天天操夜夜摸 | 成人av影视| 国产99久久| 精品中文字幕久久 | tube8欧美大屁股xxxx | 国产三级Av一区二区三区 | 国产在线可以看麻豆 | 亚洲AV无码乱码在线观看代蜜桃 | 久久不色| 日本婷婷久久久久久久久一区二区 | 亚洲国产成人精品女人久久久久 | 国产高潮流白浆视频 | 欧美一区二区三区成人久久片 | 色综合一区二区三区 | 亚洲精品AⅤ在线国自产拍 国产免费一区二区三区视频 | 自拍偷拍亚洲视频 | 中国人与拘一级毛片 | 日韩黄色毛片 | 国产亚洲一区二区手机在线观看 | 一级毛片全部免费播放特黄 | 亚洲精品国产精品乱码不99按摩 | 免费国产精品久久久久久 | av黄在线观免费网站 | 最近日本中文字幕 | 久久精品亚洲一区二区三区观看模式 | 1769中文字幕岛国 | 成人国产第一区在线观看 | 国产一区二区三区免费播放 | 成人久久av | 亚洲成av www人 | 日日碰狠狠躁久久躁 | 亚洲精品综合精品自拍 | 国产精亚洲视频 | 99久久精品国产综合一区 | 91亚洲国产成人 |