| AVS 60th International Symposium and Exhibition | |
| Biomaterial Interfaces | Thursday Sessions |
| Session BI+AS+BA+NS+SS-ThA |
| Session: | Biomolecules at Interfaces |
| Presenter: | N.P. Reynolds, CSIRO Materials Science & Engineering, Australia |
| Authors: | N.P. Reynolds, CSIRO Materials Science & Engineering, Australia K.E. Styan, CSIRO Materials Science & Engineering, Australia C. Easton, CSIRO Materials Science & Engineering, Australia R. Mezzenga, ETH Zürich, Switzerland B. Muir, CSIRO Materials Science & Engineering, Australia P. Hartley, CSIRO Materials Science & Engineering, Australia |
| Correspondent: | Click to Email |
Interactions of tissue cells with their local microenvironment (the extracellular matrix) can be split into three distinct categories: 1) Physical interactions, such as cellular responses to elasticity or stiffness, 2) chemical interactions, with specific epitopes contained within the extracellular matrix, and 3) topographical interactions with the nanoscale fibrous proteins that make up the majority of the extracellular matrix. In order to study how these interactions affect cell physiology in vitro, biomimetic substrates can be designed to reproduce these interactions. Whilst there have been multiple examples of substrates that accurately mimic chemical and physical interactions, the effects of truly biomimetic topographies are less well explored.
We show for the first time it is possible to use networks of self-assembled amyloid fibers as templates for the deposition of plasma polymers under high vacuum conditions. The nanoscale topography of the underlying amyloid networks is replicated on the top surface of the polymers with remarkable fidelity, resulting in a chemically homogenous surface with well-defined nanoscale surface features that mimic the topography of the extracellular matrix. The culture of fibroblast cells on these substrates resulted in an increased cell attachment and spreading compared to flat polymer films. We show evidence that the increase in favorable cell spreading was caused by a stabilization of adsorbed serum proteins (including fibronectin) by the nano-topography. Thus, we hypothesize that the reduced denaturation of proteins on the nano-topographical substrates results in matrix adhesion moieties (e.g. the RGD sequence) being presented to the cell membrane in a more physiological orientation. This templating technique allows for the rapid and reproducible fabrication of substrates with nanoscale biomimetic topography. We believe that such surfaces will have applications in the development of new biomaterials that will allow the routine investigation of physiological nanoscale morphology on cellular phenotype.
N.P. Reynolds et. al., "Nano-topographic surfaces with defined surface chemistries from amyloid fibril networks can control cell attachment” Biomacromolecules, 2013, DOI: 10.1021/bm400430t.