FNIII 14 Peptide TEATITGLEPGTEYTITYVIAL derives from fibronectin type III domains, containing alternating polar and hydrophobic residues. The sequence supports studies of β-sheet formation, ligand-binding surfaces, and protein-matrix interactions. Researchers employ it to map folding transitions, structural motifs, and adhesion-related properties. Its well-defined composition suits biophysical analyses.
CAT No: R2086
FNIII 14 Peptide TEATITGLEPGTEYTITYVIAL is a synthetic peptide corresponding to a specific sequence within the fibronectin type III (FNIII) domain, a structurally conserved module found in a variety of extracellular matrix proteins. The FNIII domain is recognized for its role in mediating protein-protein interactions, contributing to cellular adhesion, migration, and signaling processes. As a research tool, this peptide offers a well-defined platform for investigating the structural and functional aspects of fibronectin-related interactions, enabling exploration of mechanisms underlying cell-matrix communication and the broader dynamics of extracellular matrix biology.
Peptide-functional studies: Researchers utilize FNIII 14-derived peptides to dissect the molecular basis of cell adhesion and migration. By incorporating this sequence into in vitro assays, investigators can analyze how specific domains of fibronectin contribute to integrin binding and downstream signaling events. Such studies are instrumental in elucidating the modular roles of FNIII domains and their influence on cellular behavior, providing insights into tissue morphogenesis, wound healing, and developmental biology.
Protein interaction mapping: The defined sequence of this peptide enables its use in mapping interaction sites between fibronectin and its cellular partners. Through techniques such as surface plasmon resonance, pull-down assays, or solid-phase binding studies, the peptide facilitates identification and characterization of binding affinities with integrins, syndecans, or other extracellular matrix receptors. This approach supports the development of mechanistic models for extracellular matrix assembly and receptor-ligand specificity.
Biomaterials and surface modification: FNIII 14 peptides are frequently incorporated into biomaterial coatings to enhance cell attachment and modulate surface bioactivity. By grafting the peptide onto synthetic substrates, researchers can create environments that selectively engage cell surface receptors, promoting desired cellular responses in tissue engineering applications. This strategy aids in the rational design of scaffolds and implants that mimic natural extracellular matrix cues, supporting improved cell integration and function.
Peptide synthesis and analytical validation: The FNIII 14 sequence serves as a reference standard in peptide synthesis and analytical method development. Its well-characterized structure and sequence facilitate optimization of solid-phase peptide synthesis protocols and provide a benchmark for evaluating chromatographic or mass spectrometric performance. Laboratories engaged in custom peptide production or quality control benefit from using such defined peptides to refine purification and analytical workflows.
Signal transduction research: By employing this peptide in cell-based assays, scientists can probe the signaling pathways activated upon engagement of FNIII motifs. The peptide's interaction with specific receptors can trigger intracellular cascades, allowing for the study of downstream events such as cytoskeletal rearrangement, gene expression modulation, or kinase activation. These investigations contribute to a deeper understanding of how extracellular matrix components regulate cellular physiology and adaptative responses to the microenvironment.
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