利用力谱技术对胞吐蛋白相互作用进行单分子探测。
Single Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy.
作者信息
Montana Vedrana, Liu Wei, Mohideen Umar, Parpura Vladimir
机构信息
Department of Neurobiology, Center for Glial Biology in Medicine, Atomic Force Microscopy & Nanotechnology Laboratories, Civitan International Research Center, Evelyn F. McKnight Brain Institute, University of Alabama, Birmingham, AL 35294, USA.
出版信息
Croat Chem Acta. 2008 Apr 1;81(1):31.
Abstract
Relatively recently, the Atomic Force Microscope (AFM) emerged as a powerful tool for single molecule nanomechanical investigations. Parameters that can be measured by force spectroscopy using AFM, such as the force and total mechanical extension required to break bonds between various proteins can yield valuable insights into the nature of the bond (zippering vs. highly localized binding site), the sequence of its interactions and the energy landscape along the length of the interaction. In this review we discuss the use of AFM in force spectroscopy mode to study intermolecular interactions between the exocytotic proteins of the core SNARE complex. Information gathered by force spectroscopy of protein-protein interactions of this complex supplement previous results acquired with other techniques, and allows a deeper understanding of SNARE protein interactions and their role in exocytosis.
摘要
相对较近的时候，原子力显微镜（AFM）成为单分子纳米力学研究的强大工具。通过使用AFM的力谱学可以测量的参数，例如破坏各种蛋白质之间键所需的力和总机械伸长，能够对键的性质（拉链式与高度局部化结合位点）、其相互作用序列以及沿相互作用长度的能量景观产生有价值的见解。在本综述中，我们讨论了在力谱学模式下使用AFM来研究核心SNARE复合体的胞吐蛋白之间的分子间相互作用。通过对该复合体蛋白质-蛋白质相互作用的力谱学收集的信息补充了先前用其他技术获得的结果，并有助于更深入地理解SNARE蛋白相互作用及其在胞吐作用中的作用。
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