Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen-Binding Peptide binds fibrinogen and inhibits both the adhesion of platelets to fibrinogen and platelet aggregation, and also inhibits the adhesion of platelets to vitronectin.
CAT No: R1350
CAS No:137235-80-4
Synonyms/Alias:Fibrinogen-Binding Peptide;137235-80-4;Glu-his-ile-pro-ala;Glutamyl-histidyl-isoleucyl-prolyl-alanine;(4S)-4-amino-5-[[(2S)-1-[[(2S,3S)-1-[(2S)-2-[[(1S)-1-carboxyethyl]carbamoyl]pyrrolidin-1-yl]-3-methyl-1-oxopentan-2-yl]amino]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid;DTXSID80160116;L-Alanine, N-(1-(N-(N-L-alpha-glutamyl-L-histidyl)-L-isoleucyl)-L-prolyl)-;CHEMBL1409520;DTXCID5082607;HY-P1741;NCGC00167251-01;DA-63437;MS-30246;CS-0095106;G12502;(S)-4-amino-5-((S)-1-((2S,3S)-1-((S)-2-((S)-1-carboxyethylcarbamoyl)pyrrolidin-1-yl)-3-methyl-1-oxopentan-2-ylamino)-3-(1H-imidazol-4-yl)-1-oxopropan-2-ylamino)-5-oxopentanoic acid;
Fibrinogen-Binding Peptide is a synthetic peptide designed to selectively interact with fibrinogen, a key glycoprotein involved in blood clotting and extracellular matrix assembly. As a molecular tool, it provides researchers with a precise means to probe, modulate, or mimic fibrinogen's biological interactions in vitro and in various experimental systems. The peptide's affinity for fibrinogen enables targeted studies of coagulation pathways, cell-matrix dynamics, and the molecular mechanisms underlying hemostasis and tissue remodeling. Its defined sequence and reproducible binding properties make it valuable for applications in biochemical research, assay development, and biomaterials engineering.
Affinity-based assay development: Fibrinogen-binding peptides are widely employed in the design and optimization of affinity-based assays, such as enzyme-linked immunosorbent assays (ELISAs) and biosensor platforms. By immobilizing the peptide on solid supports or sensor surfaces, researchers can achieve specific capture or detection of fibrinogen from complex biological samples. This approach enhances assay selectivity, reduces background interference, and supports the quantitative analysis of fibrinogen in plasma, cell culture media, or tissue extracts. The peptide's high specificity also facilitates the development of competitive binding formats for screening inhibitors or modulators of fibrinogen interactions.
Cell adhesion and migration studies: The peptide serves as a functional ligand in studies investigating cell adhesion, spreading, and migration, particularly for cell types that express integrins or other fibrinogen-binding receptors. By coating culture substrates with the peptide, investigators can dissect the contribution of fibrinogen-mediated signaling to cellular behavior, cytoskeletal organization, and downstream gene expression. This enables mechanistic exploration of cell-extracellular matrix interactions in contexts such as wound healing, angiogenesis, or tumor invasion, providing insights into the molecular cues that govern tissue dynamics.
Biomaterials functionalization: In biomaterials research, fibrinogen-binding peptides are utilized to modify the surface properties of scaffolds, hydrogels, or implantable devices. Incorporation of the peptide onto material surfaces enhances their bioactivity by promoting selective adhesion of fibrinogen, which in turn can modulate subsequent cell attachment, proliferation, and tissue integration. This strategy is particularly relevant in the engineering of vascular grafts, wound dressings, or regenerative scaffolds where controlled cell-material interactions are critical for successful outcomes.
Protein-protein interaction mapping: Researchers employ the peptide as a molecular probe to map and characterize protein-protein interactions involving fibrinogen. By using the peptide in pull-down assays, crosslinking experiments, or competition studies, it is possible to identify binding partners, delineate interaction domains, and quantify binding affinities. Such studies are essential for elucidating the structural and functional determinants of fibrinogen's role in coagulation cascades, immune responses, and extracellular matrix assembly.
Inhibitor screening and drug discovery: The selective binding properties of the peptide make it a valuable tool for high-throughput screening of small molecules, antibodies, or peptides that modulate fibrinogen activity. By serving as a competitive ligand in binding assays, it enables the identification and characterization of compounds that disrupt or enhance fibrinogen interactions. This application supports early-stage drug discovery efforts targeting coagulation disorders, thrombosis, or pathological tissue remodeling, providing a robust platform for mechanistic and pharmacological investigations.
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