作者: Radha Santonocito , Francesca Venturella , Fabrizio Dal Piaz , Maria Agnese Morando , Alessia Provenzano
关键词: Recombinant DNA 、 Escherichia coli 、 Perna viridis 、 Structural biology 、 Chemistry 、 Adhesion 、 Bioadhesive 、 Biophysics 、 Cell culture 、 Mussel
摘要: During their lifecycle, many marine organisms rely on natural adhesives to attach wet surfaces for movement and self-defense in aqueous tidal environments. Adhesive proteins from mussels are biocompatible elicit only minimal immune responses humans. Therefore these have received increased attention potential applications medicine, biomaterials, biotechnology. The Asian green mussel Perna viridis secretes several byssal plaque proteins, molecules that help anchoring the surfaces. Among protein-5β (Pvfp-5β) initiates interactions with substrate, displacing interfacial water before binding surface. Here, we established first recombinant expression Escherichia coli of Pvfp-5β. We characterized Pvfp-5β, finding despite displaying a CD spectrum consistent features random coil, protein is correctly folded as indicated by MS NMR analyses. Pvfp-5β folds β-sheet–rich expected an epidermal growth factor-like module. examined effects cell viability adhesion capacity NIH-3T3 HeLa lines, revealing has no cytotoxic at concentrations used provides good cell-adhesion strength both glass plastic plates. Our findings suggest adhesive properties make it efficient surface-coating material, potentially suitable biomedical including regeneration damaged tissues.