Toggle Main Menu Toggle Search

Open Access padlockePrints

Monitoring the assembly of antibody-binding membrane protein arrays using polarised neutron reflection

Lookup NU author(s): Anton Le Brun, Professor Jeremy Lakey

Downloads

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


Abstract

Protein arrays are used in a wide range of applications. The array described here binds IgG antibodies, produced in rabbit, to gold surfaces via a scaffold protein. The scaffold protein is a fusion of the monomeric E. coli porin outer membrane protein A (OmpA) and the Z domain of Staphylococcus aureus protein A. The OmpA binds to gold surfaces via a cysteine residue in a periplasmic turn and the Z domain binds immunoglobulins via their constant region. Polarised Neutron Reflection is used to probe the structure perpendicular to the gold surface at each stage of the assembly of the arrays. Polarised neutrons are used as this provides a means of achieving extra contrast in samples having a magnetic metal layer under the gold surface. This contrast is attained without resorting to hydrogen/deuterium exchange in the biological layer. Polarised Neutron Reflection allows for the modelling of many and complex layers with good fits. The total thickness of the biological layer immobilised on the gold surface is found to be 187 Å and the layer can thus far be separated into its lipid, protein and solvent parts. © 2008 EBSA.


Publication metadata

Author(s): Le Brun AP, Holt SA, Shah DS, Majkrzak CF, Lakey JH

Publication type: Article

Publication status: Published

Journal: European Biophysics Journal

Year: 2008

Volume: 37

Issue: 5

Pages: 639-645

ISSN (print): 0175-7571

ISSN (electronic): 1432-1017

Publisher: Springer

URL: http://dx.doi.org/10.1007/s00249-008-0291-2

DOI: 10.1007/s00249-008-0291-2


Altmetrics

Altmetrics provided by Altmetric


Actions

Find at Newcastle University icon    Link to this publication


Share