Non-covalent assembly of peptide-growth factor complexes to spatially control cell activity

PMSE 128

Gregory A. Hudalla, greg.hudalla@gmail.com, Department of Biomedical Engineering, University of Wisconsin, 1550 Engineering Drive, Madison, WI 53706 and William L. Murphy, wlmurphy@wisc.edu, Department of Pharmacology, University of Wisconsin, 1550 Engineering Drive, Madison, WI 53706.
Tissue development involves a complex interplay of spatially distinct signals, including protein growth factors, leading to controlled precursor cell differentiation. Spatial control over growth factor activity in synthetic materials may enable more direct mimicry of tissue development, and may ultimately promote more effective tissue regeneration. We have developed a strategy that uses non-covalent assembly as a basis to sequester protein growth factors within materials. Our approach uses covalently immobilized “aptamers” to specifically and non-covalently bind growth factors to a material. In principle, this strategy allows us to control the concentration of local growth factor assemblies over a wide range by varying the affinity of the protein-aptamer interaction and/or the density of covalently immobilized aptamer. Our presentation will describe this strategy and other non-covalent assembly approaches designed to localize bio-macromolecules near the cell surface in 2-D and 3-D cell culture platforms.