Screening of integrin-binding peptides from the laminin α4 and α5 chain G domain peptide library

摘要: Laminins, a multifunctional protein family of extracellular matrix, interact with various types integrin. Here, integrin-mediated cell adhesive peptides have been systematically screened in the laminin α4 and α5 chain G domain peptide library consisting 211 by both peptide-coated plastic plates peptide-conjugated Sepharose bead assays using human dermal fibroblasts. Thirteen promoted spreading activity was specifically inhibited EDTA. Cell attachment to 11 anti-integrin β1 antibody. Additionally, A5G81 (AGQWHRVSVRWG) A5G84 (TWSQKALHHRVP) α3 α6 antibodies. These results suggest that promote integrin α3β1- α6β1-mediated attachment. Further, most are located loop regions domains, suggesting structure is important for specific recognition. Integrin binding useful understanding functions potential use biomaterials drug development.