Fibronectin-Laminin a1 Fusion Peptide, FN-A208

Product Name: Fibronectin-Laminin a1 Fusion Peptide, FN-A208

Sequence One Letter Code: GRGDSGAASIKVAVSADR

Sequence Three Letter Code: H-Gly-Arg-Gly-Asp-Ser-Gly-Ala-Ala-Ser-Ile-Lys-Val-Ala-Val-Ser-Ala-Asp-Arg-OH

Chemical Formula:C69H121N25O26

Molecular Weight: 1716.9

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Peptide Series

Source / Species: murine

Conjugation: Unconjugated

Code Nacres: NA.26

Application: FN-A208 is a bioactive fusion peptide composed of the A208 sequence from murine laminin α1 linked via a glycine spacer to the fibronectin-derived GRGDS integrin-binding motif. The peptide self-assembles into amyloid-like fibrils and promotes fibroblast attachment through coordinated interactions with integrins and IKVAV-binding receptors. These interactions stimulate actin stress fiber formation and cytoskeletal organization. FN-A208 is widely used in studies of cell adhesion, extracellular matrix signaling, and integrin-mediated mechanotransduction. Its bioadhesive and self-assembling properties make it particularly valuable in biomaterials and tissue regeneration research, including scaffold functionalization and engineered microenvironment design.

Current Research: The extracellular matrix (ECM) provides more than structural support for tissues—it actively regulates cell adhesion, signaling, and differentiation. Interactions between cells and ECM components such as laminin and fibronectin control essential biological processes including cytoskeletal organization, migration, and tissue regeneration. Synthetic peptides derived from ECM proteins have become valuable tools for reproducing these interactions in controlled experimental systems. FN-A208 is a bioactive fusion peptide designed to combine key functional motifs from laminin and fibronectin, enabling it to promote cell adhesion while forming organized fibrillar structures. Because of these properties, FN-A208 is widely used in studies of cell–matrix interactions, integrin signaling, and biomaterial design. Structural Design of the FN-A208 Fusion Peptide FN-A208 integrates two biologically active peptide sequences derived from extracellular matrix proteins. The first component, A208, originates from the murine laminin α1 chain, a major structural protein of basement membranes. Laminin-derived peptides are known to regulate cell adhesion and signaling by interacting with receptors that recognize laminin motifs within the ECM. The second component is the GRGDS sequence, a well-known integrin-binding motif derived from fibronectin. The RGD motif is recognized by several integrin receptors expressed on the surface of many cell types, including fibroblasts, endothelial cells, and epithelial cells. Engagement of integrins with RGD-containing ligands triggers intracellular signaling pathways that regulate cell spreading, cytoskeletal organization, and mechanotransduction. In FN-A208, the laminin-derived sequence and the GRGDS motif are connected by a glycine spacer, which provides flexibility between the two functional domains. This structural arrangement allows both motifs to remain accessible for receptor interactions, enabling the peptide to engage multiple cell-surface receptors simultaneously. Self-Assembly into Amyloid-Like Fibrils A distinctive feature of FN-A208 is its ability to self-assemble into amyloid-like fibrillar structures under suitable conditions. Peptide self-assembly occurs through noncovalent interactions such as hydrogen bonding, hydrophobic interactions, and electrostatic forces. These interactions drive the organization of peptide molecules into ordered supramolecular structures. The resulting fibrils resemble aspects of natural extracellular matrix fibers, creating a nanoscale architecture that can support cell attachment. Unlike pathological amyloid aggregates, the fibrillar structures formed by designed peptides like FN-A208 are intentionally engineered and used as functional biomaterials. The self-assembly behavior of FN-A208 provides a useful experimental platform for studying how nanostructured peptide matrices influence cellular behavior, particularly in systems that aim to replicate features of native ECM environments. Integrin-Mediated Cell Adhesion One of the primary biological functions of FN-A208 is its ability to promote fibroblast attachment. The GRGDS motif within the peptide binds integrins on the cell surface, initiating receptor-mediated adhesion. Integrins are transmembrane proteins that connect extracellular ligands to intracellular cytoskeletal networks, forming focal adhesion complexes that regulate cell shape and mechanical signaling. Simultaneously, the laminin-derived A208 segment can interact with receptors that recognize laminin-associated motifs, including those associated with IKVAV-binding pathways. These interactions provide additional adhesive signals that enhance cell–matrix communication. Through these combined receptor interactions, FN-A208 supports strong cellular attachment and promotes downstream signaling events that influence cytoskeletal dynamics. Cytoskeletal Organization and Mechanotransduction When fibroblasts attach to FN-A208 matrices, they exhibit actin stress fiber formation and cytoskeletal organization. These changes arise from integrin-mediated signaling pathways that activate intracellular regulators of actin polymerization and focal adhesion assembly. The formation of stress fibers reflects the development of tension-bearing actin bundles within the cell, which are connected to the extracellular environment through integrin receptors. This structural linkage allows cells to sense and respond to mechanical properties of their surroundings, a process known as mechanotransduction. By providing integrin-binding cues within a fibrillar peptide matrix, FN-A208 enables researchers to investigate how extracellular signals influence cellular mechanics, migration, and adhesion dynamics. Applications in Cell Adhesion and ECM Signaling Studies Because FN-A208 integrates key ECM signaling motifs and forms organized structures, it is widely used in studies of cell adhesion and extracellular matrix signaling. Researchers employ the peptide to investigate how cells interact with synthetic matrices that mimic natural ECM environments. In vitro experiments using FN-A208 help clarify how integrin engagement regulates cellular processes such as spreading, migration, and cytoskeletal remodeling. The peptide also serves as a model system for analyzing how multiple ECM-derived motifs cooperate to regulate cell behavior. These studies contribute to understanding the molecular basis of cell–matrix communication, which plays a critical role in tissue development, wound healing, and disease progression. Relevance to Biomaterials and Tissue Regeneration The self-assembling and adhesive properties of FN-A208 make it particularly useful in biomaterials research and tissue engineering. Peptide-based materials can be incorporated into scaffolds or coatings that promote cell attachment and guide tissue regeneration. In regenerative medicine, synthetic matrices that mimic ECM signals are used to create engineered microenvironments capable of supporting cell growth and differentiation. FN-A208 provides both structural and biochemical cues that can enhance cellular interactions with biomaterial surfaces. The peptide is also useful for scaffold functionalization, where it can be integrated into hydrogels, nanofibers, or other biomaterial platforms to improve bioactivity and cell compatibility. Conclusion FN-A208 represents a sophisticated example of a bioactive fusion peptide designed to replicate essential features of the extracellular matrix. By combining the laminin-derived A208 sequence with the fibronectin GRGDS integrin-binding motif, the peptide supports coordinated receptor interactions that promote fibroblast adhesion and cytoskeletal organization. Its ability to self-assemble into amyloid-like fibrils further enhances its value as a model ECM mimic, enabling studies of cell–matrix interactions and mechanotransduction within structured peptide environments. Through applications in cell adhesion research, biomaterials development, and tissue regeneration studies, FN-A208 continues to provide insights into how engineered peptide systems can influence cellular behavior and support the design of functional biomimetic materials.