Statistic Copolymers Working as Growth Factor-Binding Mimics of Fibronectin

Growth factors (GFs) play important roles in biological system and are widely used in tissue regeneration. However, their application is greatly hindered by short in vivo lifetime of GFs. GFs are bound to fibronectin dynamically in the extracellular matrix, which inspired the authors to mimic the GF binding domain of fibronectin and design GF-binding amphiphilic copolymers bearing positive charges. The optimal amino acid polymer can bind to a variety of representative GFs, such as bone morphogenetic protein-2 (BMP-2) and TGF-beta 1 from the transforming growth factor-beta superfamily, PDGF-AA and PDGF-BB from the platelet-derived growth factor family, FGF-10 and FGF-21 from the fibroblast growth factor family, epidermal growth factor from the EGF family and hepatocyte growth factor from the plasminogen-related growth factor family, with binding affinities up to the nanomolar level. 3D scaffolds immobilized with the optimal copolymer enable sustained release of loaded BMP-2 without burst release and significantly enhances the in vivo function of BMP-2 for bone formation. This strategy opens new avenues in designing GF-binding copolymers as synthetic mimics of fibronectin for diverse applications.

Automated summary

Growth factors play crucial roles in tissue regeneration, but their short in vivo lifetime limits their application. Researchers have designed amphiphilic copolymers with positive charges, mimicking the GF binding domain of fibronectin, to improve the stability and function of growth factors by enhancing their binding affinities to a wide range of representative growth factors.