Arg-Gly-Asp, sequence involved in cell adhesion, is an integrin-binding site and belongs to the class of adhesion proteins. It can be used as a brain tumor-targeting ligand.
CAT No: 10-101-268
CAS No:2378808-45-6
Synonyms/Alias:RGD Trifluoroacetate;2378808-45-6;RGD (Trifluoroacetate);(S)-2-(2-((S)-2-Amino-5-guanidinopentanamido)acetamido)succinic acid trifluoroacetate;(2S)-2-[[2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]butanedioic acid;2,2,2-trifluoroacetic acid;poly(rgd); trifluoroacetic acid;HY-P0278A;BS-47702;CS-0040825;E75473;2-[[2-[[2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]butanedioic acid;2,2,2-trifluoroacetic acid;
Arg-Gly-Asp (TFA salt) is a synthetic tripeptide composed of the amino acids arginine, glycine, and aspartic acid, presented in its trifluoroacetic acid salt form. Recognized for its central role as the canonical RGD motif, this peptide sequence is a critical recognition site for various integrin receptors that mediate cell adhesion to the extracellular matrix. The RGD sequence is highly conserved across multiple extracellular proteins, making it a fundamental tool for investigating cell-matrix interactions, integrin binding specificity, and signal transduction pathways. Its biochemical relevance extends to a wide range of research fields, including cell biology, biomaterials science, and molecular pharmacology, where precise modulation of cell adhesion and migration is essential for experimental design and functional studies.
Cell adhesion studies: The RGD peptide is widely utilized as a molecular probe to study integrin-mediated cell adhesion. By incorporating the tripeptide into in vitro assays, researchers can selectively inhibit or promote the attachment of various cell types to substrates, thereby dissecting the roles of specific integrin receptors. This approach enables detailed characterization of cell-extracellular matrix interactions, providing insights into adhesion dynamics, receptor-ligand specificity, and downstream signaling events relevant to tissue development, wound healing, and pathological processes such as metastasis.
Surface functionalization in biomaterials research: Functionalization of biomaterial surfaces with the RGD motif is a well-established strategy to enhance cellular compatibility and direct cell behavior in tissue engineering applications. Immobilizing the peptide onto synthetic scaffolds, hydrogels, or implant surfaces facilitates integrin engagement, thereby promoting cell attachment, spreading, and proliferation. This technique is instrumental in developing advanced biomaterials that mimic native extracellular environments and support the growth and differentiation of various cell types for regenerative medicine and in vitro tissue models.
Receptor binding assays: The Arg-Gly-Asp sequence serves as a competitive ligand in integrin binding assays, allowing for the quantitative analysis of receptor-ligand interactions. By competing with endogenous matrix proteins for integrin occupancy, the peptide enables the assessment of binding affinities, receptor selectivity, and the functional consequences of integrin engagement. Such assays are critical for screening potential integrin antagonists, mapping binding domains, and elucidating molecular mechanisms underlying cell signaling events associated with adhesion.
Cell migration and invasion models: Researchers employ the RGD tripeptide to modulate and investigate cellular migration and invasion in various experimental systems. By altering the availability of the motif in the extracellular environment or blocking integrin function, the peptide can be used to dissect the molecular pathways that govern directional cell movement. These studies are particularly valuable in understanding processes such as embryonic development, immune cell trafficking, and tumor cell dissemination, where regulated migration is fundamental.
Peptide-based drug delivery research: The RGD motif is increasingly explored as a targeting ligand in the design of peptide-based drug delivery systems. By conjugating the sequence to nanoparticles, liposomes, or other carrier platforms, researchers can exploit its integrin-binding properties to achieve selective delivery of bioactive agents to cells expressing specific integrin subtypes. This targeted approach enhances cellular uptake and internalization, facilitating the development of more effective and selective delivery vehicles for experimental therapeutics in preclinical research settings.
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