RGD Peptides

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CAT# Product Name M.W Molecular Formula Inquiry
10-101-267 Arg-Gly-Asp 346.34 C12H22N6O6 Inquiry
10-101-316 SDGRG 490.5 C17H30N8O9 Inquiry
F1411 GGGGRGDS 661.6 Inquiry
R04002 TP508, Thrombin-derived Peptide 2312.5 Inquiry
R04003 GRGDS, amide 489.5 Inquiry
R04004 RGDfV 574.6 C26H38N8O7 Inquiry
R04007 GRGDTP 601.6 Inquiry
R04008 GRGESP 601.6 Inquiry
R04011 GRADSPK 729.8 Inquiry
R04012 RGDyK Inquiry
R04013 RGDyC Inquiry
R04015 RADyK Inquiry
R04016 E(RGDyK)2 Inquiry
R04017 RGD - 4C 1145.3 Inquiry
R04018 Prototype of RGD - containing peptide, FITC - labeled 1091.6 Inquiry
R04020 Ac-Asp-Arg-Gly-Asp-Ser-OH 590.55 Inquiry
R04022 Ac-Pen-Arg-Gly-Asp-Cys-OH 620.71 Inquiry
R04023 Bifunctional Antiplatelet Agent 1298.56 Inquiry
R04024 Cyclo(-Ala-Arg-Gly-Asp-3-aminomethylbenzoyl) 532.56 Inquiry
R04025 Cyclo(-Arg-Ala-Asp-D-Phe-Cys) 592.68 Inquiry

Introduction

The RGD peptides is a small peptide containing three amino acids of arginine-glycine-aspartate (Arg-Gly-Asp), which is widely distributed in various organisms and various tissues of the same organism. The RGD sequence is an essential component in a variety of biological extracellular matrices and plasma protein structures, and studies have found that RGD sequences are also present on the cell surface. RGD, a short tripeptide, acts as an important cell recognition site and signaling promoter and plays an important regulatory role in many life activities. RGD, as a recognition site for integrin interaction with its ligand, can specifically bind to 11 integrins, thereby promoting a series of physiological behaviors such as adhesion, migration, infiltration, and proliferation between cells and between cells and extracellular matrix.

Mechanism of action

The RGD peptides are capable of interacting with the cell integrin receptor integrin αυβ3. RGD peptides can destroy the signaling pathway between thyroid hormone and integrin, prevent the interaction of thyroid hormone and integrin to inhibit the activation of MMP-9, and ultimately inhibit the growth and invasion of multiple myeloma cells. RGD peptides completely prevent the transfer of polymorphonuclear cells on the surface of cultured human vascular endothelial cells, so RGD peptides can significantly inhibit SNB-19 and T98G tumor cells (glioblastoma cell line) against fibronectin and vitronectin. Adhesion and the adhesion activity of tumor cells to extracellular matrix plays an important role in local invasion of glioblastoma cells. In addition, RGD activates caspase-9, caspase-8, and caspase-3, and suggests that molecules involved in mitochondria and Fas-dependent pathways are involved in the induction of tumor cell apoptosis.

Application of RGD peptides

As a site of action of integrin and integrin ligands, RGD sequences play an extremely important role in the diagnosis and treatment of tumors. RGD peptides alone can cause tumor cell apoptosis, together with other anti-tumor drugs or methods. When used, it can increase the therapeutic effect of the tumor. In addition, RGD peptides act as a drug delivery vehicle in the process of targeting tumor cells.

References

  1. Kitayama, J., Hidemura, A., Saito, H., & Nagawa, H. (2000). Shear stress affects migration behavior of polymorphonuclear cells arrested on endothelium. Cellular immunology, 203(1), 39-46.
  2. Anuradha, C. D., Kanno, S., & Hirano, S. (2000). RGD peptide-induced apoptosis in human leukemia HL-60 cells requires caspase-3 activation. Cell biology and toxicology, 16(5), 275-283.
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