Toggle Main Menu Toggle Search

Open Access padlockePrints

Self-assembling layers created by membrane proteins on gold

Lookup NU author(s): Dr Deepan Shah, Anton Le Brun, Professor Jeremy LakeyORCiD

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Abstract

Membrane systems are based on several types of organization. First, amphiphilic lipids are able to create monolayer and bilayer structures which may be flat, vesicular or micellar. Into these structures membrane proteins can be inserted which use the membrane to provide signals for lateral and orientational organization. Furthermore, the proteins are the product of highly specific self-assembly otherwise known as folding, which mostly places individual atoms at precise places in three dimensions. These structures all have dimensions in the nanoscale, except for the size of membrane planes which may extend for millimetres in large liposomes or centimetres on planar surfaces such as monolayers at the air/water interface. Membrane systems can be assembled on to surfaces to create supported bilayers and these have uses in biosensors and in electrical measurements using modified ion channels. The supported systems also allow for measurements using spectroscopy, surface plasmon resonance and atomic force microscopy. By combining the roles of lipids and proteins, highly ordered and specific structures can be self-assembled in aqueous solution at the nanoscale. ©2007 Biochemical Society.


Publication metadata

Author(s): Shah DS, Thomas MB, Phillips S, Cisneros DA, Le Brun AP, Holt SA, Lakey JH

Publication type: Conference Proceedings (inc. Abstract)

Publication status: Published

Conference Name: Conference on Bionanotechnology - From Self-Assembly to Cell Biology

Year of Conference: 2007

Pages: 522-526

ISSN: 0300-5127

Publisher: Biochemical Society Transactions, Portland Press Ltd.

URL: http://dx.doi.org/10.1042/BST0350522

DOI: 10.1042/BST0350522

PubMed id: 17511643

Library holdings: Search Newcastle University Library for this item

ISBN: 14708752


Share