Anastasia Mardilovich1, Jennifer Craig2, Matthew McCammon1, Ashish Garg1, and Efrosini Kokkoli1. (1) Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN 55455, (2) Department of Biomedical Engineering, University of Minnesota, Minneapolis, MN 55455
The α5β1 integrin has been implicated in dynamic processes such as mediating adenovirus infection, accelerating wound healing, suppressing tumor recurrence and metastasis in certain cases of cancer, and providing a protection mechanism against Alzheimer's disease. Therefore, the interaction of α5β1 with its ligand, fibronectin, supports numerous adhesive functions and has an important role in health and disease. In recent years there is a considerable effort in designing fibronectin-mimicking peptides that will target the integrin with increased therapeutic potentials. However, to date, the therapeutic use of these peptides has been limited as they cannot accurately mimic fibronectin's binding affinity for α5β1. We have recently designing a peptide-amphiphile that outperforms fibronectin in terms of cell adhesion, cell spreading, cytoskeletal organization, and extracellular matrix protein production. The focus of this presentation will be our biomimetic studies (collective and single-molecule atomic force microscopy interactions in a biomimetic cell-free system, and in vitro cell studies) that led to the designing of this novel peptide-amphiphile.