The adsorption of proteins onto interfaces and surfaces, for example the air-water and oil-water interfaces, is central to a number of biological processes and applications in biotechnology. Absorption of proteins onto such interfaces is typically associated with changes in protein conformation, often with a consequent loss of function. Obtaining a detailed molecular description of this structural change is a key step to understanding protein structure and function in complex environments.

In this talk I will describe some recent work aimed at investigating adsorption and conformational change of proteins at liquid interfaces. Specifically the adsorption of hydrophobins, amphiphilic proteins onto oil-water interfaces will be discussed [1]. Using coarse-grained simulations the adsorption strength of two examples of these proteins has been determined and related to their surface structure. The conformations adopted by two peptides derived from myoglobin, for which the emulsification behaviour has been studied experimentally [2], will also be discussed. Both peptides adopt similar, compact conformations in bulk solution and readily adsorb onto the air-water interface [3], where they show different interfacial conformations. I will also discuss the investigation of fibronectin adsorption onto polymer surfaces using a combination of computational and experimental techniques.

[1] D. L. Cheung, Langmuir, 28, 8730 (2012)

[2] S. Poon, A. E. Clarke, and C. J. Schultz, J. Coll. Interf. Sci., 213, 193 (1999)

[3] D. L. Cheung, Langmuir, 32, 4405 (2016)

[4] D. Mallinson et al, J. Biomed. Mater. Res. A, in press (http://onlinelibrary.wiley.com/doi/10.1002/jbm.a.35949/full)