A nonenzymatic chemiluminescent reaction enabling chemiluminescence resonance energy transfer to quantum dots.
A nonenzymatic chemiluminescent reaction enabling chemiluminescence resonance energy transfer to quantum dots.
复制标题
DOI：
10.1002/chem.201000478
复制
发表时间：
2010-06-01
影响因子：
4.3
通讯作者：
Liu, Yi-Ming
中科院分区：
文献类型：
--
作者：
Zhao, Shulin;Huang, Yong;Liu, Rongjun;Shi, Ming;Liu, Yi-Ming
基于共振能量转移（RET）的测量方法对于创新研究非常有用，例如具有空间和/或时间分辨率的活细胞中蛋白质-蛋白质相互作用[1]。RET涉及紧邻（通常< 10 nm）的供体和受体之间的非辐射（偶极-偶极）能量转移。发生在两个荧光团之间的RET被称为荧光RET（FRET），而发生在发光供体酶（例如荧光素酶）和荧光团之间的RET被称为生物发光RET（BRET）。已经看到许多关于FRET用于各个领域的出版物，例如生物大分子的结构解析、它们的相互作用、体外测定、体内监测和活细胞中的信号转导[2，3]。BRET也是一种对这些研究有用的技术[4，5]。BRET的主要缺点包括需要至少一种精心设计的蛋白质融合体和低发射强度，这损害了BRET测量中的空间和/或时间分辨率。化学发光RET（CRET）涉及能量从发光（CL）供体（而不是BRET中的生物发光酶供体）到荧光团受体的非辐射转移[6]。CRET通过CL化合物的氧化发生，然后激发荧光受体。由于在CRET方法中不使用外部光源进行激发，因此可以最小化在FRET测量中经常观察到的由外部光激发引起的非特异性信号。与BRET相比，基于CRET的方法不涉及蛋白质融合。CL供体和荧光受体均可与抗体偶联，具有广泛的应用前景。然而，到目前为止，关于CRET的研究很少[6-8]。一个主要的困难是确定一个有效的CL供体或反应，可以激发荧光受体的能量转移。在以往的CRET工作中，均采用辣根过氧化物酶（HRP）催化的鲁米诺-H_2O_2化学发光反应。不幸的是，涉及外源酶（即HRP）限制了CRET系统的适用性。在许多情况下，它使测定复杂化，例如，干扰所研究的生物相互作用。
Resonance energy transfer (RET)-based measurement approaches are very useful for innovative studies such as that of protein-protein interactions in living cells with spatial and/or temporal resolution [1]. RET involves non-radiative (dipole-dipole) energy transfer between a donor and an acceptor that are in close proximity (normally< 10 nm). RET that occurs between two fluorophores is known as fluorescence RET (FRET), whereas RET that occurs between a light-emitting donor enzyme (eg luciferase) and a fluorophore is known as bioluminescence RET (BRET). Numerous publications have been seen on FRET being used in various areas such as structural elucidation of biological macromolecules, their interactions, in vitro assays, in vivo monitoring, and signal transduction in living cells [2, 3]. BRET is also well documented as a technique useful for these studies [4, 5]. Major disadvantages of BRET include the requirement of at least one carefully designed protein fusion and the low emission intensity that compromises the spatial and/or temporal resolutions in BRET measurements. Chemiluminescence RET (CRET) involves nonradiative transfer of energy from a chemiluminescent (CL) donor (instead of a bioluminescent enzyme donor as in BRET) to a fluorophore acceptor [6]. CRET occurs by the oxidation of a CL compound that then excites the fluorescent acceptor. Since no external light source is used for excitation in CRET approaches, nonspecific signals caused by external light excitation as often observed in FRET measurements can be minimized. Compared with BRET, a CRET-based approach involves no protein fusion. Both the CL donor and fluorescent acceptor can be conjugated to antibodies, promising a widespread application. However, little study has been so far reported on CRET [6-8]. A major difficulty is to identify an effective CL donor or reaction that can excite a fluorescent acceptor by energy transfer. In all of the previous CRET works reported, the luminol-H2O2 CL reaction catalyzed by horseradish peroxidase (HRP) was used. Unfortunately, involving an exogenous enzyme (ie HRP) limits the applicability of the CRET system. In many cases, it complicates the assay by, for example, disturbing the biological interactions under study.
登录
查看更多内容
影响因子：
29.4
作者：
Li, J;Hong, X;Li, TJ
通讯作者：
Li, TJ
基于生物发光共振能传递的生物传感和成像。
影响因子：
7.7
作者：
Xia, Zuyong;Rao, Jianghong
通讯作者：
Rao, Jianghong
影响因子：
7.4
作者：
Shi, Lifang;Rosenzweig, Nitsa;Rosenzweig, Zeev
通讯作者：
Rosenzweig, Zeev
影响因子：
41.2
作者：
Zhang, CY;Yeh, HC;Wang, TH
通讯作者：
Wang, TH
量子点量子产率对化学发光共振能量转移的影响
影响因子：
6.2
作者：
Wang, Hai-Qiao;Li, Yong-Qiang;Zhao, Yuan-Di
通讯作者：
Zhao, Yuan-Di