Nanoscale presentation of cell adhesive molecules via block copolymer self-assembly

• Published in: Biomaterials 2009-09, Vol.30 (27), p.4732-4737
• Main Authors: George, Peter A, Doran, Michael R, Croll, Tristan I, Munro, Trent P, Cooper-White, Justin J
• Format: Article
• Language: English
• Subjects: Advanced Basic Science; Animals; Biological Assay; Cell Adhesion Molecules - metabolism; Cell spreading; Dentistry; Fibroblasts - cytology; Fibroblasts - ultrastructure; Integrin; Magnetic Resonance Spectroscopy; Maleimides; Mice; Microscopy, Atomic Force; Microscopy, Fluorescence; Nanostructures - chemistry; Nanotechnology; NIH 3T3 Cells; Polyethylene Glycols - chemistry; Polyethylene Glycols - metabolism; Polystyrenes - chemistry; Polystyrenes - metabolism; RGD; Surface modification; Surface Properties
• ISSN: 0142-9612; 1878-5905
• DOI: 10.1016/j.biomaterials.2009.05.039

Abstract Precise control over the nanoscale presentation of adhesion molecules and other biological factors represents a new frontier for biomaterials science. Recently, the control of integrin spacing and cellular shape has been shown to affect fundamental biological processes, such as differentiation and apoptosis. Here, we present the self-assembly of maleimide functionalised polystyrene-block-poly (ethylene oxide) copolymers as a simple, yet highly precise method for controlling the position of cellular adhesion molecules. By manipulating the phase separation of the functional PS-PEO block copolymer used in this study, via a simple blending technique, we alter the nanoscale (on PEO domains of 8–14 nm in size) presentation of the adhesion peptide, GRGDS, decreasing lateral spacing from 62 nm to 44 nm and increasing the number density from ∼450 to ∼900 islands per μm2 . The results indicate that the spreading of NIH-3T3 fibroblasts increases as the spacing between domains of RGD binding peptides decreases. Further, the same functional PS-PEO surfaces have been utilised to immobilise, via a zinc chelating peptide sequence, poly-histidine tagged proteins and extracellular matrix (ECM) fragments. This method is seen as an ideal platform for investigations into the role of spatial arrangements of cell adhesion molecules and ECM molecules on cell function and, in particular, control of cell phenotype.