Title

Label-Free Measuring And Mapping Of Binding Kinetics Of Membrane Proteins In Single Living Cells

Department

neurobiology

Document Type

Article

Abstract

Membrane proteins mediate a variety of cellular responses to extracellular signals. Although membrane proteins are studied intensively for their values as disease biomarkers and therapeutic targets, in situ investigation of the binding kinetics of membrane proteins with their ligands has been a challenge. Traditional approaches isolate membrane proteins and then study them ex situ, which does not reflect accurately their native structures and functions. We present a label-free plasmonic microscopy method to map the local binding kinetics of membrane proteins in their native environment. This analytical method can perform simultaneous plasmonic and fluorescence imaging, and thus make it possible to combine the strengths of both label-based and label-free techniques in one system. Using this method, we determined the distribution of membrane proteins on the surface of single cells and the local binding kinetic constants of different membrane proteins. Furthermore, we studied the polarization of the membrane proteins on the cell surface during chemotaxis. © 2012 Macmillan Publishers Limited. All rights reserved.

Publication Date

10-1-2012

Publication Title

Nature Chemistry

ISSN

17554330

Volume

4

Issue

10

First Page

846

Last Page

853

Digital Object Identifier (DOI)

10.1038/nchem.1434

This document is currently not available here.

Share

COinS