Using Neutron Reflectometry to Characterize Antimicrobial Protein Surface Coatings

2017 ◽  
Vol 121 (24) ◽  
pp. 5908-5916 ◽  
Author(s):  
Peter W. Akers ◽  
Andrew J. Dingley ◽  
Simon Swift ◽  
Andrew R. J. Nelson ◽  
Julie Martin ◽  
...  
Keyword(s):  
Neutron Reflectometry ◽  
Surface Coatings ◽  
Antimicrobial Protein ◽  
Protein Surface

scholarly journals Polymer and protein surface coatings on silicone: effect on Staphylococcus epidermidis adhesion and colonization

2006 ◽  
Vol 3 (S1) ◽  
Author(s):  
KY Simon Ng ◽  
Haiying Tang ◽  
Ting Cao ◽  
Anfeng Wang ◽  
Xuemei Liang ◽  
...  
Keyword(s):  
Staphylococcus Epidermidis ◽  
Surface Coatings ◽  
Protein Surface

Unravelling the structural complexity of protein–lipid interactions with neutron reflectometry

2021 ◽  
Author(s):  
Luke A. Clifton
Keyword(s):  
Structural Information ◽  
Biological Membrane ◽  
Structural Complexity ◽  
Neutron Reflectometry ◽  
Antimicrobial Protein ◽  
Relative Distribution ◽  
Buried Structures ◽  
Lipid Interactions ◽  
Low Energies ◽  
Before And After

Neutron reflectometry (NR) is a large-facility technique used to examine structure at interfaces. In this brief review an introduction to the utilisation of NR in the study of protein–lipid interactions is given. Cold neutron beams penetrate matter deeply, have low energies, wavelengths in the Ångstrom regime and are sensitive to light elements. High differential hydrogen sensitivity (between protium and deuterium) enables solution and sample isotopic labelling to be utilised to enhance or diminish the scattering signal of individual components within complex biological structures. The combination of these effects means NR can probe buried structures such as those at the solid–liquid interface and encode molecular level structural information on interfacial protein–lipid complexes revealing the relative distribution of components as well as the overall structure. Model biological membrane sample systems can be structurally probed to examine phenomena such as antimicrobial mode of activity, as well as structural and mechanistic properties peripheral/integral proteins within membrane complexes. Here, the example of the antimicrobial protein α1-purothionin binding to a model Gram negative bacterial outer membrane is used to highlight the utilisation of this technique, detailing how changes in the protein/lipid distributions across the membrane before and after the protein interaction can be easily encoded using hydrogen isotope labelling.

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