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Using membrane stress to our advantage

Using membrane stress to our advantage
Using membrane stress to our advantage
The nature of the bilayer motif coupled with the ability of lipids and proteins to diffuse freely through this structure is crucial to the viability of cells and their ability to compartmentalize domains contained therein. It seems surprising to find then that biological as well as model membranes exist in a dynamic state of mechanical stress. The stresses within such membranes are surprisingly large, typically reaching up to 50 atm (1 atm=101.325 kPa) at the core of the membrane and vary as a function of depth. The uneven distribution of lateral pressures within monolayer leaflets causes them to bend away from or towards the water interface. This can result in the formation of complex, self-assembled mesophases, many of which occur in vivo. Our knowledge of the principles underlying membrane mechanics has reached the point where we are now able to manipulate them and create nano-structures with reasonable predictability. In addition, they can be used both to explain and control the partitioning of amphipathic proteins on to membranes. The dependence of the dynamics of membrane-bound proteins and the chemical reactivity of amphipathic drug molecules on membrane stresses suggests that Nature itself takes advantage of this. Understanding and manipulating these internal forces will be a key element in creating self-assembled, biocompatible, nanoscale cell-like systems.
curvature, frustration, diglucosyldiacylglycerol synthase, ctp-phosphocholine cytidylyltransferase, binding, acholeplasma-laidlawii, cubic phases, cationic amphiphilic drug, bilayer, phase, behaviour, ctp: phosphocholine, membrane stress, cytidylyltransferase (cct), lipid-bilayer, lipid polymorphism, water-systems, membranes, phase-transition
0300-5127
498-501
Shearman, G.C.
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Attard, G.S.
3219075d-2364-4f00-aeb9-1d90f8cd0d36
Hunt, A.N.
95a3e223-da96-40e7-b47d-27dce014e305
Jackowski, S.
7338eae6-4c3a-4a75-abe0-aa2abbf70560
Baciu, M.
1cca0f03-a675-42b7-b1b0-933f5f8bb7c5
Sebai, S.C.
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Mulet, X.
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Clarke, J.A.
175f7a42-4f09-41a8-a7ce-bb58b4c439e3
Law, R.V.
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Plisson, C.
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Parker, C.A.
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Gee, A.
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Ces, O.
c698a6a8-166b-47ec-a1ac-f46aaab8c5cb
Templer, R.H.
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Shearman, G.C.
2a39e357-ce78-48f9-81d4-a798c6b0bdba
Attard, G.S.
3219075d-2364-4f00-aeb9-1d90f8cd0d36
Hunt, A.N.
95a3e223-da96-40e7-b47d-27dce014e305
Jackowski, S.
7338eae6-4c3a-4a75-abe0-aa2abbf70560
Baciu, M.
1cca0f03-a675-42b7-b1b0-933f5f8bb7c5
Sebai, S.C.
a4c17d7d-fe43-45fe-8402-38999cac932f
Mulet, X.
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Clarke, J.A.
175f7a42-4f09-41a8-a7ce-bb58b4c439e3
Law, R.V.
19a53f44-610d-480a-b86a-aa8bacc37acf
Plisson, C.
adf616c0-dd48-4071-b432-bd92b23554ee
Parker, C.A.
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Gee, A.
66278a26-5f70-4d60-951b-66c286c4d9ff
Ces, O.
c698a6a8-166b-47ec-a1ac-f46aaab8c5cb
Templer, R.H.
10946a6b-8333-4d2a-9607-e9d04973d4c2

Shearman, G.C., Attard, G.S., Hunt, A.N., Jackowski, S., Baciu, M., Sebai, S.C., Mulet, X., Clarke, J.A., Law, R.V., Plisson, C., Parker, C.A., Gee, A., Ces, O. and Templer, R.H. (2007) Using membrane stress to our advantage. Biochemical Society Transactions, 35, 498-501.

Record type: Article

Abstract

The nature of the bilayer motif coupled with the ability of lipids and proteins to diffuse freely through this structure is crucial to the viability of cells and their ability to compartmentalize domains contained therein. It seems surprising to find then that biological as well as model membranes exist in a dynamic state of mechanical stress. The stresses within such membranes are surprisingly large, typically reaching up to 50 atm (1 atm=101.325 kPa) at the core of the membrane and vary as a function of depth. The uneven distribution of lateral pressures within monolayer leaflets causes them to bend away from or towards the water interface. This can result in the formation of complex, self-assembled mesophases, many of which occur in vivo. Our knowledge of the principles underlying membrane mechanics has reached the point where we are now able to manipulate them and create nano-structures with reasonable predictability. In addition, they can be used both to explain and control the partitioning of amphipathic proteins on to membranes. The dependence of the dynamics of membrane-bound proteins and the chemical reactivity of amphipathic drug molecules on membrane stresses suggests that Nature itself takes advantage of this. Understanding and manipulating these internal forces will be a key element in creating self-assembled, biocompatible, nanoscale cell-like systems.

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More information

Published date: 2007
Keywords: curvature, frustration, diglucosyldiacylglycerol synthase, ctp-phosphocholine cytidylyltransferase, binding, acholeplasma-laidlawii, cubic phases, cationic amphiphilic drug, bilayer, phase, behaviour, ctp: phosphocholine, membrane stress, cytidylyltransferase (cct), lipid-bilayer, lipid polymorphism, water-systems, membranes, phase-transition

Identifiers

Local EPrints ID: 54384
URI: http://eprints.soton.ac.uk/id/eprint/54384
ISSN: 0300-5127
PURE UUID: 58e36c0b-795c-45f1-be34-b51fb67bcf90
ORCID for G.S. Attard: ORCID iD orcid.org/0000-0001-8304-0742
ORCID for A.N. Hunt: ORCID iD orcid.org/0000-0001-5938-2152

Catalogue record

Date deposited: 31 Jul 2008
Last modified: 09 Jan 2022 02:47

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Contributors

Author: G.C. Shearman
Author: G.S. Attard ORCID iD
Author: A.N. Hunt ORCID iD
Author: S. Jackowski
Author: M. Baciu
Author: S.C. Sebai
Author: X. Mulet
Author: J.A. Clarke
Author: R.V. Law
Author: C. Plisson
Author: C.A. Parker
Author: A. Gee
Author: O. Ces
Author: R.H. Templer

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