In the past several years, researchers have been building increasingly sophisticated surfaces to tailor the interactions between synthetic materials and biochemical systems.
It is now well established that the ordering and presentation of surface ligands on the micro- to nano-scale is important in biological systems. Recent studies suggest that proteins bind differently to nano-patterned materials, the concept that is increasingly being used for design of novel materials and devices for biomedical applications. However, at present, there are few guiding principles for the design and study of interactions between proteins and nano-structured surfaces. Although general considerations of electrostatics and hydrophobicity can adequately describe some single component or well-mixed systems, more detailed descriptions are needed for molecular-level patterned interfaces. Due to the complexity of probing organic hydrated systems at the nanoscale, it is likely that a combination of experiments and computer simulation will be needed to explore such systems.
Prof. Molly Stevens from Imperial College London conducts pioneering ground breaking engineering of nanomaterials for drug delivery and tissue replacement technologies. RMIT University has developed a capability to model the functionalised nanoparticles and protein dynamics on the surfaces of those nanoparticles. In our first joint investigation we have recently demonstrated that amphiphilic amino acids can play a crucial role in specific adsorption behaviour proteins on monolayer protected gold nanoparticles. Using atomistic simulations we identified that amphipilic amino acids can bind simultaneously to both the hydrophobic and hydrophilic surface domains due to their dual nature and size compatibility with the nanostructured surfaces.
- Amphiphilic amino acids: a key to adsorbing proteins to nanopatterned surfaces?, A. Hung, M. Mager, M. Hembury, F. Stellacci, M. M. Stevens, I.Yarovsky, Chem. Sci., 4 (2013) 928 - 937, Edge article featured on the front cover.
- Ordering Surfaces on the Nanoscale: implications for protein adsorption, A. Hung, S. Mwenifumbo, M. Mager, J. Kuna, M. Hembury, F. Stellacci, I. Yarovsky and M. M. Stevens, Journal of the American Chemical Society, 133 (5) (2011) 1438–1450
- Nanoparticles in biological environment: insights from simulations, I. Yarovsky, N. Todorova, A. Hung, A. Makarucha, International Congress on Theoretical Biophysics, TheoBio 2011, Madeira, Portugal, June 2011
- Effects of nanodomain structure on protein-surface binding,Andrew Hung, Steve Mwenifumbo, Matthew Hembury, Molly Stevens, Jeffrey Kuna, Francesco Stellacci and Irene Yarovsky, 35th Lorne Conference on Protein Structure and Function, Australia, February 2010
- Protein interactions with monolayer-protected nanoparticles, Andrew Hung, Steve Mwenifumbo, Matthew Hembury, Molly Stevens, Jeffrey Kuna, Francesco Stellacci and Irene Yarovsky, Australian Biophysics Society (ABS) meeting, Ballarat, 29 Nov- 2 Dec 2009