862772-11-0

Basic information

• Product Name: Cyclo(-Arg-Gly-Asp-D-Phe-Cys)
• Synonyms: Cyclo(-Arg-Gly-Asp-D-Phe-Cys);Cyclo(-RGDfC), avb3 Integrin Binding Cyclic RGD Peptide;Cyclo(-RGDfC), avb3 Integrin Binding Cyclic RGD Peptide, c(RGDfC);Cyclo(-Arg-Gly-Asp-D-Phe-Cys) Acetate salt;c(RGDfC),cyclo(Arg-Gly-Asp-d-Phe-Cys)
• CAS NO: 862772-11-0
• Molecular Formula: C₂₄H₃₄N₈O₇S
• Molecular Weight: 578.64
• Mol File: 862772-11-0.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Density: 1.55±0.1 g/cm3(Predicted)
• PKA: 4.01±0.10(Predicted)
• CAS DataBase Reference: Cyclo(-Arg-Gly-Asp-D-Phe-Cys)(CAS DataBase Reference)
• NIST Chemistry Reference: Cyclo(-Arg-Gly-Asp-D-Phe-Cys)(862772-11-0)
• EPA Substance Registry System: Cyclo(-Arg-Gly-Asp-D-Phe-Cys)(862772-11-0)

Safety Data

• Hazardous Substances Data: 862772-11-0(Hazardous Substances Data)

Usage

Description

Cyclo(-Arg-Gly-Asp-D-Phe-Cys), also known as Cyclo(L-arginylglycyl-L-α-aspartyl-D-phenylalanyl-L-cysteinyl), is a peptide molecule with a cyclic structure. It is composed of five amino acids, including arginine, glycine, aspartic acid, phenylalanine, and cysteine. This cyclic peptide has unique properties that make it a promising candidate for various applications, particularly in the field of cancer research and therapy.

Uses

Used in Cancer Research and Therapy:
Cyclo(-Arg-Gly-Asp-D-Phe-Cys) is used as a targeting agent for cancer-targeted drug delivery. It can be conjugated with hyperbranched amphiphilic block copolymers to enhance the specificity and efficiency of drug delivery to cancer cells. This approach allows for the selective delivery of therapeutic agents to tumor sites, reducing side effects and improving treatment outcomes.
Used in Non-Invasive Imaging Techniques:
Cyclo(-Arg-Gly-Asp-D-Phe-Cys) is also used in non-invasive positron emission tomography (PET) imaging for tumor detection and monitoring in tumor-bearing mice. The conjugation of this cyclic peptide with imaging agents enables the visualization of tumor sites and the assessment of treatment efficacy, providing valuable information for the development of personalized cancer therapies.

Upstream product

• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 103213-32-7 N-(9-fluorenylmethoxycarbonyl)-S-trityl-L-cysteine 
• 86123-10-6 Fmoc-D-Phe-OH 
• 187618-60-6 Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine 
• 19767-45-4 mesna 

Downstream Products

• 1261036-95-6 C₆₇H₉₀N₁₀O₁₆S₂ 
• 1261036-96-7 C₁₁₁H₁₅₅N₂₃O₂₈S₃ 
• 1616835-65-4 cabazitaxel 

Relevant articles and documents

A Facile N-Mercaptoethoxyglycinamide (MEGA) Linker Approach to Peptide Thioesterification and Cyclization

The C-terminal electrophilic activation of peptides by α-thioesterification requires strongly acidic conditions or complex chemical manipulations, which ultimately limit functional group compatibility and broad utility. Herein, we report a readily accessible N-mercaptoethoxyglycinamide (MEGA) solid-phase linker for the facile synthesis of latent peptide α-thioesters. Incubating peptide-MEGA sequences with 2-mercaptoethanesulfonic acid at mildly acidic pH yielded α-thioesters that were directly used in NCL without purification. The MEGA linker yielded robust access to thioesters ranging in length from 4 to 35 amino acids, and greatly simplified the synthesis of cyclic peptides. Finally, the high utility of MEGA was demonstrated by the one-pot synthesis of a functional analog of the Sunflower Trypsin Inhibitor 1.

Multimerization of cRGD peptides by click chemistry: Synthetic strategies, chemical limitations, and influence on biological properties

Integrin αvβ3 is overexpressed on endothelial cells of growing vessels as well as on several tumor types, and so integrin-binding radiolabeled cyclic RGD pentapeptides have attracted increasing interest for in vivo imaging of αvβ3 integrin expression by positron emission tomography (PET). Of the cRGD derivatives available for imaging applications, systems comprising multiple cRGD moieties have recently been shown to exhibit highly favorable properties in relation to monomers. To assess the synthetic limits of the cRGD-multimerization approach and thus the maximum multimer size achievable by using different efficient conjugation reactions, we prepared a variety of multimers that were further investigated in vitro with regard to their avidities to integrin αvβ3. The synthesized peptide multimers containing increasing numbers of cRGD moieties on PAMAM dendrimer scaffolds were prepared by different click chemistry coupling strategies. A cRGD hexadecimer was the largest construct that could be synthesized under optimized reaction conditions, thus identifying the current synthetic limitations for cRGD multimerization. The obtained multimeric systems were conjugated to a new DOTA-based chelator developed for the derivatization of sterically demanding structures and successfully labeled with 68Ga for a potential in vivo application. The evaluated multimers showed very high avidities-increasing with the number of cRGD moieties-in in vitro studies on immobilized αvβ3 integrin and U87MG cells, of up to 131-and 124-fold, respectively, relative to the underivatized monomer.