Biological Activities of Integrin-binding Peptides Derived from Laminins on Alginate and Chitosan Matrices

摘要

Basement membrane (BM), a thin extracellular matrix (ECM), plays a critical role in tissue regeneration and remodeling. The major components of BM are type IV collagen, laminin, perlecan, and nidogen. Of them, laminins are heterotrimeric basement membrane proteins, consisting of α,β, and y chains and exhibit multiple biological functions through interactions with other matrix molecules and with cell surface receptors. The regulation of these interactions is critical for many biological processes, including promotion of cell adhesion, migration, neurite outgrowth, angiogenesis, and wound healing. Matrigel, an extract of BM derived from mouse sarcoma, has been widely used as a three-dimensional cell culture matrix, but it is not possible to apply for human. Our goal is to develop a synthetic Matrigel and use for tissue engineering. Previously, we screened active sequences from laminin. We synthesized more than 3000 peptides, and identified many active peptides. It is expected that the active peptides from laminin are applied to biomedical field, but their application has been limited due to their short half-life in the body. Therefore, it has been required to have stable peptides of long-lasting activity that directly affect cells in the tissues. So far, natural' polysaccharides, including alginate and chitosan, have been used as a biomaterial. In our-previous studies, we conjugated the laminin active peptides to polysaccharides, alginate and chitosan matrices and demonstrated their usefulness for cell transplantation and cell culture.