Advanced

Hydrodynamic trapping measures the interaction between membrane-associated molecules

Junghans, Victoria LU ; Hladilkova, Jana LU ; Santos, Ana Mafalda; Lund, Mikael LU ; Davis, Simon J. and Jönsson, Peter LU (2018) In Scientific Reports 8(1).
Abstract

How membrane proteins distribute and behave on the surface of cells depends on the molecules’ chemical potential. However, measuring this potential, and how it varies with protein-to-protein distance, has been challenging. Here, we present a method we call hydrodynamic trapping that can achieve this. Our method uses the focused liquid flow from a micropipette to locally accumulate molecules protruding above a lipid membrane. The chemical potential, as well as information about the dimensions of the studied molecule, are obtained by relating the degree of accumulation to the strength of the trap. We have used this method to study four representative proteins, with different height-to-width ratios and molecular properties; from globular... (More)

How membrane proteins distribute and behave on the surface of cells depends on the molecules’ chemical potential. However, measuring this potential, and how it varies with protein-to-protein distance, has been challenging. Here, we present a method we call hydrodynamic trapping that can achieve this. Our method uses the focused liquid flow from a micropipette to locally accumulate molecules protruding above a lipid membrane. The chemical potential, as well as information about the dimensions of the studied molecule, are obtained by relating the degree of accumulation to the strength of the trap. We have used this method to study four representative proteins, with different height-to-width ratios and molecular properties; from globular streptavidin, to the rod-like immune cell proteins CD2, CD4 and CD45. The data we obtain illustrates how protein shape, glycosylation and flexibility influence the behaviour of membrane proteins, as well as underlining the general applicability of the method.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scientific Reports
volume
8
issue
1
publisher
Nature Publishing Group
external identifiers
  • scopus:85051864016
ISSN
2045-2322
DOI
10.1038/s41598-018-30285-0
language
English
LU publication?
yes
id
160ac899-8dd4-4d4e-ace3-1900595556bb
date added to LUP
2018-09-05 14:28:10
date last changed
2019-02-20 11:25:47
@article{160ac899-8dd4-4d4e-ace3-1900595556bb,
  abstract     = {<p>How membrane proteins distribute and behave on the surface of cells depends on the molecules’ chemical potential. However, measuring this potential, and how it varies with protein-to-protein distance, has been challenging. Here, we present a method we call hydrodynamic trapping that can achieve this. Our method uses the focused liquid flow from a micropipette to locally accumulate molecules protruding above a lipid membrane. The chemical potential, as well as information about the dimensions of the studied molecule, are obtained by relating the degree of accumulation to the strength of the trap. We have used this method to study four representative proteins, with different height-to-width ratios and molecular properties; from globular streptavidin, to the rod-like immune cell proteins CD2, CD4 and CD45. The data we obtain illustrates how protein shape, glycosylation and flexibility influence the behaviour of membrane proteins, as well as underlining the general applicability of the method.</p>},
  articleno    = {12479},
  author       = {Junghans, Victoria and Hladilkova, Jana and Santos, Ana Mafalda and Lund, Mikael and Davis, Simon J. and Jönsson, Peter},
  issn         = {2045-2322},
  language     = {eng},
  month        = {12},
  number       = {1},
  publisher    = {Nature Publishing Group},
  series       = {Scientific Reports},
  title        = {Hydrodynamic trapping measures the interaction between membrane-associated molecules},
  url          = {http://dx.doi.org/10.1038/s41598-018-30285-0},
  volume       = {8},
  year         = {2018},
}