Fibronectin Adhesion-Promoting Peptide

Fibronectin Adhesion-Promoting Peptide is a synthetic research peptide in the fibronectin-derived cell-adhesion peptide family. Fibronectin contains multiple cell- and protein-binding domains. The RGD motif in the cell-binding region is a foundational integrin-recognition sequence, while other fibronectin-derived motifs can display different receptor preferences. Fibronectin fragments and analogs are useful for integrin binding, cell adhesion, matrix assembly, biomaterial functionalization, and structure-activity experiments.

• receptor or ligand-binding assays
• competition studies
• biochemical or enzymatic assays
• analytical LC-MS/HPLC methods
• antibody controls
• cell-based experiments
• comparative structure-activity studies

For a fragment, residue-substituted analog, stereochemical variant, labeled peptide, or terminally modified form, experimental behavior should be evaluated for the exact construct rather than assumed to match the native parent peptide. Sequence-dependent solubility, aggregation, adsorption, oxidation, and stability should be considered when establishing reconstitution, storage, and assay conditions.

1. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
2. Isolation of a highly specific ligand for the alpha5 beta1 integrin from a phage display library