Biopolymers and supramolecular polymers as biomaterials for biomedical applications
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Introduction The extracellular matrix (ECM) is present within all tissues and organs; it provides mechanical support and both guides and directs cell function.1 The ECM is composed of two main classes of macromolecules: proteoglycans and fibrous proteins, with distinct hierarchical assemblies at various length scales.2,3 The hierarchical structure–function relationship of these biopolymers regulates the functions of cells, tissues, and organs. In the context of biomaterials for regenerative medicine, proteins that can be used to construct scaffolds that mimic the structure and function of the ECM are of particular interest.4 Specifically, fibrillar proteins that are abundant components of the native ECM, such as collagen and fibronectin (FN), are natural choices for tissue engineering applications.5–7 Collagen is responsible for the structural support and elasticity of tissues.8 FN supports cell adhesion to the ECM, as well as cell migration, proliferation, and differentiation.9,10 In addition to collagen and FN, silk proteins (originating from silkworms and spiders) have attracted considerable interest for tissue engineering applications because of their tailorable mechanical properties, good biocompatibility, and facile processability.11–13 Critical to the function of these and other protein biopolymers is their
ability to spontaneously assemble from smaller subunits into long uniform structures stabilized by many noncovalent interactions. In some cases, the dynamic features of these interactions are coupled with the capacity of the resulting fibrillar structures to rapidly polymerize and depolymerize and guide specific function through biomechanical and biochemical signals.14–16 The intracellular fibers known collectively as the cell’s cytoskeleton are the best example of the central functional role of highly dynamic fibrous structures. The hierarchical self-assembly of proteins into well-defined structures has inspired research on artificial supramolecular architectures intended to mimic the function of native proteins. In these supramolecular assemblies, the monomeric units are held together by multiple noncovalent intermolecular interactions such as hydrogen bonding,17–20 metal–ligand coordination,21–23 π–π stacking,24 hydrophobic interactions,25 and host–guest interactions.26,27 Unlike covalent polymerization, all of these processes are highly reversible and dynamic, thus endowing the new polymer materials with many attractive properties. Such properties include a structurally responsive nature, easy synthesis and functionalization, and the possibility of incorporating an array of different ligands through co-assembly of
Ronit Freeman, Simpson Querrey Institute of BioNanotechnology, Northwestern University, USA; [email protected] Job Boekhoven, Institute for Advanced Study and Chemistry Department, Technische Universität Munchen, Germany; [email protected] Matthew B. Dickerson, Materials and Manufacturing Directorate, Air Force Research Laboratory, USA; [email protected] Rajesh R. Naik, 711th Hum
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