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G-protein-coupled receptor screening technologies.G蛋白偶联受体筛选技术
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Unique agonist-bound cannabinoid CB1 receptor conformations indicate agonist specificity in signaling.独特的激动剂结合型大麻素CB1受体构象表明信号传导中的激动剂特异性。
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Structural basis of function in heterotrimeric G proteins.异源三聚体G蛋白功能的结构基础
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Functional selectivity and classical concepts of quantitative pharmacology.功能选择性与定量药理学的经典概念。
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Ligand modulation of lateral segregation of a G-protein-coupled receptor into lipid microdomains in sphingomyelin/phosphatidylcholine solid-supported bilayers.在鞘磷脂/磷脂酰胆碱固体支持双层膜中，配体对G蛋白偶联受体侧向分离进入脂质微区的调节作用。
Biochemistry. 2005 Jun 28;44(25):9168-78. doi: 10.1021/bi050207a.
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Plasmon-waveguide resonance studies of lateral segregation of lipids and proteins into microdomains (rafts) in solid-supported bilayers.固体支撑双层膜中脂质和蛋白质横向分离成微区（筏）的表面等离子体激元 - 波导共振研究
J Biol Chem. 2005 Mar 25;280(12):11175-84. doi: 10.1074/jbc.M411197200. Epub 2005 Jan 24.
7
Selectivity, cooperativity, and reciprocity in the interactions between the delta-opioid receptor, its ligands, and G-proteins.δ-阿片受体、其配体与G蛋白之间相互作用的选择性、协同性和互惠性。
J Biol Chem. 2004 Oct 22;279(43):44673-82. doi: 10.1074/jbc.M404713200. Epub 2004 Aug 17.
8
Different structural states of the proteolipid membrane are produced by ligand binding to the human delta-opioid receptor as shown by plasmon-waveguide resonance spectroscopy.如表面等离子体波导共振光谱所示，配体与人类δ阿片受体结合会产生蛋白脂质膜的不同结构状态。
Mol Pharmacol. 2004 May;65(5):1248-57. doi: 10.1124/mol.65.5.1248.
9
Graphical analysis of mass and anisotropy changes observed by plasmon-waveguide resonance spectroscopy can provide useful insights into membrane protein function.通过表面等离子体波导共振光谱法观察到的质量和各向异性变化的图形分析可为膜蛋白功能提供有用的见解。
Biophys J. 2004 Apr;86(4):2508-16. doi: 10.1016/S0006-3495(04)74306-4.
10
Plasmon-waveguide resonance studies of ligand binding to the human beta 2-adrenergic receptor.配体与人β2-肾上腺素能受体结合的表面等离子体波导共振研究。
Biochemistry. 2004 Mar 23;43(11):3280-8. doi: 10.1021/bi035825a.

表面等离子体波导共振（PWR）光谱法用于直接观察G蛋白偶联受体（GPCR）/G蛋白相互作用的速率并定量亲和力。

Plasmon-waveguide resonance (PWR) spectroscopy for directly viewing rates of GPCR/G-protein interactions and quantifying affinities.

作者信息

Hruby Victor J, Tollin Gordon

机构信息

Department of Chemistry, University of Arizona, Tucson, AZ 85721, USA.

出版信息

Curr Opin Pharmacol. 2007 Oct;7(5):507-14. doi: 10.1016/j.coph.2007.08.001. Epub 2007 Sep 14.

DOI:10.1016/j.coph.2007.08.001
PMID:17869585
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2151673/
Abstract

Plasmon-waveguide resonance (PWR) spectroscopy is an optical technique that has been developed in our laboratories and applied to the study of membrane-associated proteins, especially GPCRs. It has high sensitivity and requires no labeling of materials, and it can monitor changes in proteolipid mass density and conformation in real time using plasmon excitation by light polarized both perpendicular and parallel to the resonator surface. Direct measurements will be described of the association of ligands and G-proteins to GPCRs incorporated into a self-assembled lipid bilayer deposited on the silica surface of a PWR resonator. These studies have provided new insights into the functioning of this important class of signaling proteins.

摘要

表面等离子体波导共振（PWR）光谱学是一种我们实验室开发的光学技术，已应用于膜相关蛋白的研究，尤其是G蛋白偶联受体（GPCRs）。它具有高灵敏度，无需对材料进行标记，并且可以通过与谐振器表面垂直和平行偏振的光进行表面等离子体激元激发，实时监测蛋白脂质质量密度和构象的变化。将描述对结合到沉积在PWR谐振器二氧化硅表面的自组装脂质双层中的GPCRs的配体和G蛋白结合的直接测量。这些研究为这类重要信号蛋白的功能提供了新的见解。