The biological activity of extracellular matrix mimetic elastin‐like polypeptide‐laminin α1 peptide

Abstract

The extracellular matrix (ECM) is comprised of a large network of proteins essential for providing a physical scaffold as well as biochemical and biomechanical signals for tissue development and repair. Laminins are a major component of the ECM and have a diverse set of biological roles such as cell adhesion, migration, proliferation and differentiation. Laminin α1 chain bioactive RGD containing peptide, A99 (AGTFALRGDNPQG), which was previously identified to promote strong cell attachment has demonstrated utility for cell adhesion applications. A wide array of biomaterials has been created to be used as scaffolds for these types of bioactive peptides, but many are not suited for various reasons such as scalability, convenient reaction conditions or lack of homogeneity. Here, we are the first to describe methods for preparing chemically conjugated and recombinant A99 to elastin‐like polypeptides (ELPs) as the scaffold and characterize their behavior as well as evaluate the coating efficiency, cell attachment and spreading activity. These data suggest that the A99‐ELP fusion has great potential for use as a biomaterial in cell culture applications as they greatly promote cell adhesion and spreading. ELPs are biocompatible protein‐polymers that are thermo‐responsive and self‐assemble in response to heat. Below the lower critical solution temperature (LCST), they are highly soluble but above the LCST, ELPs phase separate, forming coacervates. They provide an excellent structural framework for bioactive peptides and their intrinsic biophysical characteristics allow for simple production with high yields and purity making them an ideal biomaterial for cell adhesion applications.Support or Funding InformationThis research is sponsored by the Japan Society for the Promotion of Science (JSPS), PE18045.