The development of biomimetic surfaces for protein and peptide adsorptions is continuously expanding. Their biological functions can be influenced by the properties of the underlying artificial environment but the detailed mechanism is still not clear. In the past 30 years, neutron reflectometry has been widely applied to characterise the molecular structure of proteins or multi-protein complexes and their interactions with fluid artificial membrane that mimics the cellular environment. The specific interactions, bindings or structural changes between proteins and membranes play a crucial role in cellular response sand have promising potential in diagnostics and other biosensor applications.This chapter presents the progression of surface design for protein adsorption/interactions on membranes in detail, ranging from a simple phospholipid monolayer setup to more complicated artificial lipid bilayer systems. Furthermore, a new development of designed surfaces for studying the integral membrane protein system is also discussed in this chapter. A brief overview of various membrane mimetic surfaces is first outlined, followed by presenting specific examples of protein-membrane interactions studied by neutron reflectometry. The author demonstrates how to use neutron reflectometry as anadvanced technique to provide step-by-step structural details for biomolecular applications in a well-controlled manner.
- Neutron reflectometry
- Biomimetic surfaces
- Artificial membrane
Yeung, J. C. I., Lin, T-W., & Shen, H-H. (2016). Neutron reflectometry for studying proteins/peptidesin biomimetic membranes. In W. Alfredo Monterio (Ed.), Neutron Scattering (pp. 127-148). In-Tech. https://doi.org/10.5772/62781