Cell Adhesive Peptide [RGDC]

Product Name: Cell Adhesive Peptide [RGDC]

Sequence One Letter Code: RGDC

Sequence Three Letter Code: H-Arg-Gly-Asp-Cys-OH

Cas No: 109292-46-8

Chemical Formula:C15H27N7O7S

Molecular Weight: 449.5

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: cell-adhesive peptide

SMILES: C(C[C@@H](C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)O)N)CN=C(N)N

IUPAC: (3S)-3-[[2-[[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[(1R)-1-carboxy-2-sulfanylethyl]amino]-4-oxobutanoic acid

INCHIKEY: AEGSIYIIMVBZQU-CIUDSAMLSA-N

INCHI:

InChI=1S/C15H27N7O7S/c16-7(2-1-3-19-15(17)18)12(26)20-5-10(23)21-8(4-11(24)25)13(27)22-9(6-30)14(28)29/h7-9,30H,1-6,16H2,(H,20,26)(H,21,23)(H,22,27)(H,24,25)(H,28,29)(H4,17,18,19)/t7-,8-,9-/m0/s1

Source / Species: synthetic

Conjugation: Unconjugated

Code Nacres: NA.26

Application: RGDC is a short cell-adhesive peptide containing the integrin-recognition motif RGD, which mediates binding to integrin receptors involved in cell adhesion and signaling. The terminal cysteine provides a thiol group for covalent conjugation to biomaterial surfaces via thiol-reactive chemistries, including attachment to zirconium alkoxide complexes. Immobilized RGDC promotes cell attachment, spreading, and cytoskeletal organization, particularly in human osteoblasts. This peptide is widely used in biomaterials engineering, surface functionalization, and tissue regeneration research. It enables controlled investigation of integrin-mediated adhesion, mechanotransduction, and cell–matrix interactions in engineered environments.

Current Research: The ability of cells to interact with their surrounding environment is fundamental to tissue development, regeneration, and cellular signaling. Central to these interactions are integrins, a family of transmembrane receptors that mediate adhesion between cells and the extracellular matrix (ECM). Many ECM proteins—including fibronectin, vitronectin, and laminin—contain short peptide motifs that integrins recognize to initiate cell attachment and downstream signaling. Among these motifs, the Arg-Gly-Asp (RGD) sequence is one of the most widely studied and utilized in biomaterials research. Short synthetic peptides containing this motif have become essential tools for engineering cell-responsive surfaces. One example is RGDC, a compact cell-adhesive peptide that combines the integrin-recognition sequence with a terminal cysteine to enable efficient immobilization on biomaterial surfaces. The Biological Significance of the RGD Motif The RGD sequence was originally identified as the minimal integrin-binding motif present in several extracellular matrix proteins. Integrins such as αvβ3, α5β1, and αvβ5 recognize this tripeptide sequence and use it to anchor cells to the extracellular matrix. Once engaged, integrins cluster and form focal adhesion complexes that link the extracellular environment to the intracellular cytoskeleton. This connection allows cells to sense mechanical cues and activate signaling pathways that regulate proliferation, differentiation, migration, and survival. Because of its central role in cell adhesion, the RGD motif has been widely adopted in biomaterial surface modification strategies. Incorporating RGD-containing peptides into synthetic materials allows researchers to mimic natural ECM interactions and promote controlled cellular responses. These peptides are particularly valuable in environments where native extracellular matrix proteins are absent or difficult to control. Structural Features and Design of RGDC RGDC is a short synthetic peptide composed of the integrin-recognition motif RGD followed by a cysteine residue. The addition of the terminal cysteine is a strategic modification that expands the peptide’s utility in surface engineering applications. The cysteine side chain contains a reactive thiol (-SH) group, which can participate in a variety of covalent conjugation reactions. This thiol functionality allows RGDC to be immobilized onto biomaterial surfaces through thiol-reactive chemistries, including maleimide coupling, disulfide exchange reactions, and coordination with metal-containing compounds. One notable example is its attachment to zirconium alkoxide complexes, which can serve as anchoring sites for thiol-containing ligands. Through these chemical linkages, RGDC can be stably integrated into engineered materials while maintaining accessibility of the RGD motif for integrin binding. This design provides two key advantages: Precise orientation and immobilization of the adhesive motif on surfaces. Stable covalent attachment, ensuring long-term functionality in biological environments. Promoting Cell Attachment and Cytoskeletal Organization Once immobilized on a surface, RGDC acts as a bioactive ligand for integrin receptors, enabling cells to attach and spread. When integrins bind to the RGD sequence, they cluster and recruit intracellular adaptor proteins that link the receptor complex to the actin cytoskeleton. This process leads to the formation of focal adhesions, which serve as signaling hubs regulating cellular behavior. In experimental systems, surfaces functionalized with RGDC have been shown to promote cell adhesion, spreading, and cytoskeletal organization. These effects are particularly well documented in human osteoblasts, the bone-forming cells responsible for synthesizing and mineralizing bone matrix. Osteoblast attachment to biomaterial surfaces is a crucial step in bone regeneration and implant integration. By facilitating integrin-mediated adhesion, RGDC-modified surfaces can support osteoblast morphology, encourage actin filament organization, and promote cellular activities associated with tissue formation. These properties make the peptide valuable in studies aimed at improving the biocompatibility and performance of bone-related biomaterials. Applications in Biomaterials and Tissue Engineering RGDC has become a widely used component in biomaterials engineering and surface functionalization strategies. Researchers frequently incorporate this peptide into polymers, hydrogels, metal oxide coatings, and other engineered substrates to create cell-interactive environments. Because the peptide is small and chemically defined, it offers greater control compared with full-length ECM proteins. In tissue engineering, RGDC-modified materials are used to regulate how cells attach to scaffolds and how they organize within three-dimensional structures. This is particularly important for applications such as bone regeneration, where controlled cell adhesion can influence tissue formation and scaffold integration. Another important application involves the study of cell–matrix interactions and mechanotransduction. Integrins do more than simply anchor cells—they transmit mechanical forces between the extracellular matrix and the cytoskeleton. By precisely controlling the density and spatial distribution of RGD motifs on engineered surfaces, researchers can investigate how cells respond to mechanical cues and how these signals influence differentiation and tissue development. Enabling Controlled Studies of Integrin Signaling Because RGDC provides a defined and tunable adhesive signal, it enables controlled experimental systems for studying integrin-mediated signaling pathways. Scientists can vary peptide density, surface chemistry, and substrate stiffness to examine how integrin engagement affects cell behavior. These studies contribute to a deeper understanding of how cells interpret their microenvironment and how physical and biochemical signals integrate to regulate cellular function. In summary, the RGDC peptide represents a simple yet powerful tool for biomaterials research. By combining the widely recognized RGD integrin-binding motif with a reactive cysteine residue for surface conjugation, RGDC enables precise functionalization of engineered materials. Its ability to promote integrin-mediated adhesion and cytoskeletal organization makes it valuable for investigations into cell–matrix interactions, mechanotransduction, and tissue regeneration. As biomaterials research continues to advance, peptides like RGDC will remain essential components for designing cell-responsive interfaces and studying the molecular basis of cellular adhesion.