Dr Rebecca Green

	Contact details
	Telephone	+44 (0) 118 378 8446
	Fax	+44 (0) 118 378 6331
	E-mail	rebecca.green@reading.ac.uk
	Location	School of Pharmacy, University of Reading, PO Box 228, Whiteknights, Reading, RG6 6AJ, UK

Background

Dr. R. J. Green joined the School of Chemistry in 2003 as a Lecturer in Physical Chemistry and has recently moved to the new school of Pharmacy as Lecturer in Pharmaceutics. She has established a research group in biophysical surface chemistry.  Her research concentrates on probing protein interactions at interfaces, with applications in biomaterial research and food/pharmaceutical colloid stabilisation.

Research Activities

Peptide interactions at membrane surfaces   

Antimicrobial peptides act as defensive or offensive agents by rupturing the membranes of target cells.  Some preference for bacterial cells is observed and therefore they are studied due to their potential role as a family of antibiotics.  However, their specificity towards bacterial cells varies and the mechanism for specificity is not clearly understood.  To determine the lipid layer and peptide characteristics that influence peptide-membrane interactions, our research utilises a range of complementary techniques; external reflection FTIR, surface tensiometry, atomic force microscopy and neutron reflectivity.  Using these techniques, the binding and structural changes of the peptide to lipid monolayers at the air-liquid interface and lipid bilayers at the solid-liquid interface is studied.  The composition of the lipid layer can be varied so as to model a variety of different cell types and, thus, determine the physical and chemical factors that control binding.

Protein – surfactants interactions

The study of interactions between protein and low molecular weight surfactants has importance in several biotechnological disciplines.  For example, the protein-surfactant interaction controls colloidal stability in foods and pharmaceutics, is made use of in SDS-polyacrylamide electrophoresis and controls detergency efficiency.  Our research utilises isothermal titration calorimetry, FTIR spectroscopy, surface tensiometry and neutron reflectivity to probe these interactions and to study the formation of protein-surfactant complexes in solution and at interfaces.  Recent research has focused on the interfacial structure of protein-surfactant complexes and the mechanism by which different surfactants remove protein from interfaces.  

Protein adsorption to biomaterials

Different interfacial chemistries, protein structures and solution environments all influence the way in which proteins adsorb.  Surface analytical techniques, such as neutron reflectivity and surface plasmon resonance, are used to determine how these variables control protein adsorption.  Of particular importance is a protein’s structure at the surface of cells or in contact with synthetic biological implants, since this often determines the function of the protein and/or the implant.  Spectroscopic techniques, such as Fourier transform infrared spectroscopy (FTIR), can be used to determine the changes in protein secondary structure.

 

Selected Publications

1.   “Unfolding and intermolecular association in globular proteins adsorbed at interfaces” Green RJ, Hopkinson I, Jones RAL. Langmuir 1999; 15: 5102–5110.     

2.   “Interaction of lysozyme and sodium dodecyl sulfate at the air-liquid interface” Green RJ, Su TJ, Joy H, Lu JR. Langmuir 2000; 16: 5797-5805.

3.   “The displacement of pre-adsorbed protein with a cationic surfactant at the SiO₂-water interface” Green RJ, Su TJ, Lu JR, Penfold J J. Phys. Chem. B 2001; 105: 9331-9338.

4.   “Analysis of the SDS-lysozyme binding isotherm” Lad MD, Ledger VM, Briggs B, Frazier RA, Green RJ Langmuir 2003; 19: 5098-5103.

5.   “Probing protein-tannin interactions by isothermal titration calorimetry” Frazier RA, Papadopoulou A, Kissoon D, Mueller-Harvey I, Green RJ J. Agric. Food. Chem. 2003; 5151: 5189-5195

 

All publications