130878-68-1

Basic information

• Product Name: FMOC-VAL-OSU
• Synonyms: CarbaMic acid, [1-[[(2,5-dioxo-1-pyrrolidinyl)oxy]carbonyl]-2-Methylpropyl]-, 9H-fluoren-9-ylMethyl ester, (S)-;L-Valine, N-[(9H-fluoren-9-ylmethoxy)carbonyl]-,2,5-dioxo-1-pyrrolidinyl ester;N-Fmoc-L-valine N-succinimidyl ester;Fmoc-L-valineN-hydroxysuccinimide ester≥ 99% (HPLC);FMOC-L-VALINE N-HYDROXYSUCCINIMIDE ESTER;FMOC-VAL-OSU;FMOC-VALINE-OSU;NALPHA-9-Fluorenylmethoxycarbonyl-L-valine N-hydroxysuccinimide ester
• CAS NO: 130878-68-1
• Molecular Formula: C₂₄H₂₄N₂O₆
• Molecular Weight: 436.46
• Product Categories: Amino Acids;Fmoc-Amino Acids and Derivatives;Fmoc-Amino acid series
• Mol File: 130878-68-1.mol

Chemical Properties

• Appearance: Off-white to white/Powder
• Density: 1.352 g/cm³
• Refractive Index: 1.626
• Storage Temp.: Store at 0°C
• PKA: 10.09±0.46(Predicted)
• Water Solubility: Slightly soluble in water.
• CAS DataBase Reference: FMOC-VAL-OSU(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-VAL-OSU(130878-68-1)
• EPA Substance Registry System: FMOC-VAL-OSU(130878-68-1)

Safety Data

• Safety Statements: 24/25
• Hazardous Substances Data: 130878-68-1(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
FMOC-VAL-OSU is used as a reagent for the synthesis of peptides in the pharmaceutical industry. Its application is crucial in the development of new drugs and therapies, as it aids in the formation of peptide bonds, which are the building blocks of proteins.
Used in Research and Development:
In the research and development sector, FMOC-VAL-OSU is employed as a key component in the synthesis of various peptide-based compounds. This allows scientists to explore the potential of these compounds in treating various diseases and conditions.
Used in Chemical Synthesis:
FMOC-VAL-OSU is also used in chemical synthesis, where it serves as an intermediate or building block for the creation of more complex molecules. This application is essential in the development of new materials and compounds with specific properties and functions.

InChI:InChI=1/C24H24N2O6/c1-14(2)22(23(29)32-26-20(27)11-12-21(26)28)25-24(30)31-13-19-17-9-5-3-7-15(17)16-8-4-6-10-18(16)19/h3-10,14,19,22H,11-13H2,1-2H3,(H,25,30)/t22-/m0/s1

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 68858-20-8 Fmoc-Val-OH 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 72-18-4 L-valine 

Downstream Products

• 923926-28-7 2-[3-(tert-butyl-diphenyl-silanyloxy)-propyl]-oxazolidine-3-carboxylic acid 4-{2-[2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-methyl-butyrylamino]-propionylamino}-benzyl ester 
• 159858-21-6 (S)-2-((S)-2-((((9H-fluoren-9-yl)-methoxy)carbonyl)amino)-3-methylbutanamido)-5-ureidopentanoic acid 
• 1166834-72-5 C₅₅H₅₃N₇O₁₂ 
• 1037795-30-4 C₃₇H₄₅N₅O₇ 
• 160885-98-3 2-[(S)-(fluoren-9-ylmethoxycarbonyl)amino]-3-methylbutan-1-ol 
• 863971-53-3 (9H-fluoren-9-yl)methyl ((S)-3-methyl-1-(((S)-1-((4-((((4-nitrophenoxy)carbonyl)oxy)methyl)phenyl)amino)-1-oxo-5-ureidopentan-2-yl)amino)-1-oxobutan-2-yl)carbamate 
• 159858-22-7 (9H-fluorenyl)methyl ((S)-1-(((S)-1-(((4-(hydroxymethyl)phenyl)amino)-1-oxo-5-ureidovalerylamido-2-yl)amino))-3-methylbutyramido-2-yl)-carbamate 
• 1394238-91-5 (9H-fluoren-9-yl)methyl ((S)-1-(((S)-1-((4-(hydroxymethyl)phenyl)amino)- 1-oxopropan-2-yl)amino)-3-methyl-1-oxobutan-2-yl)carbamate 
• 1394238-92-6 (9H-fluoren-9-yl)methyl ((S)-3-methyl-1-(((S)-1-((4-((((4-nitrophenoxy)carbonyl)oxy)methyl)phenyl)amino)-1-oxopropan-2-yl)amino)-1-oxobutan-2-yl)carbamate 
• 1394238-94-8 H₂N-Val-Ala-PABC-DOXO 
• 1394238-95-9 EMC-Val-Ala-PABC-DOXO 
• 1432969-78-2 C₃₈H₄₈N₄O₇ 
• 1432969-86-2 C₂₃H₃₈N₄O₅ 
• 1432970-34-7 C₄₃H₇₄N₄O₁₇ 

Relevant articles and documents

Aldehyde capture ligation for synthesis of native peptide bonds

Chemoselective reactions for amide bond formation have transformed the ability to access synthetic proteins and other bioconjugates through ligation of fragments. In these ligations, amide bond formation is accelerated by transient enforcement of an intramolecular reaction between the carboxyl and the amine termini of two fragments. Building on this principle, we introduce an aldehyde capture ligation that parlays the high chemoselective reactivity of aldehydes and amines to enforce amide bond formation between amino acid residues and peptides that are difficult to ligate by existing technologies.

Synthesis, characterization, and targeted chemotherapy of SCT200-linker-monomethyl auristatin E conjugates

Antibody-drug conjugates (ADCs) are currently among the most successful and important strategies for treating patients with solid tumors. ADCs are composed of a monoclonal antibody and warhead, which are conjugated via a linker. Currently, monomethyl auristatin E (MMAE) is the most widely applied warhead in the development of ADCs. However, MMAE-based ADCs are generally constructed using the MC-VC-PABC linker, and this design has limited structural diversity and some disadvantages. Accordingly, in this study, we generated three types of novel linker-MMAE (with alterations in the spacer, catabolizing area, and self-immolative compared with MC-VC-PABC-MMAE) in ADCs, termed SCT200-linker-MMAE conjugates, and then evaluated the linker-drug plasma stability and the rate of drug release by cathepsin B. The binding ability, internalization rates, and efficacy of all SCT200-linker-MMAE ADCs were systematically studied, and the expression of apoptosis-associated proteins and the therapeutic efficacies of SCT200-M-2, -C-2, and -C-4 were evaluated. The results showed that the activities of some of these ADCs were increased for epidermal growth factor receptor-positive tumors. Moreover, the novel linkers designed in this study can be linked with other antibodies to treat other types of cancer. Overall, these findings provide important insights into the application of SCT200-based linkers in ADCs.

Isostearyl Mixed Anhydrides for the Preparation of N-Methylated Peptides Using C-Terminally Unprotected N-Methylamino Acids

Sustainable and efficient manufacturing methods for N-methylated peptides remain underexplored despite growing interest in therapeutic N-methylated peptides within the pharmaceutical industry. A methodology for the coupling of C-terminally unprotected N-methylamino acids mediated by an isostearic acid halide (ISTAX) and silylating reagent has been developed. This approach allows for the coupling of a wide variety of amino acids and peptides in high yields under mild conditions without the need for a C-terminal deprotection step in the process of C-terminal elongation. These advantages make this a useful synthetic method for the production of peptide therapeutics and diagnostics containing N-methylamino acids.

Novel cathepsin B-sensitive paclitaxel conjugate: Higher water solubility, better efficacy and lower toxicity

In order to realize the targeted delivery of paclitaxel (PTX) to tumor through an environment-sensitive mechanism, increase its solubility in water and reformulate without toxic excipients, a novel PTX conjugate, PEG-VC-PABC-PTX was designed and synthesiz

Hydrogelation and self-assembly of Fmoc-tripeptides: Unexpected influence of sequence on self-assembled fibril structure, and hydrogel modulus and anisotropy

The self-assembly and hydrogelation properties of two Fmoc-tripeptides [Fmoc = N-(fluorenyl-9-methoxycarbonyl)] are investigated, in borate buffer and other basic solutions. A remarkable difference in self-assembly properties is observed comparing Fmoc-VLK(Boc) with Fmoc-K(Boc)LV, both containing K protected by Nε-tert-butyloxycarbonate (Boc). In borate buffer, the former peptide forms highly anisotropic fibrils which show local alignment, and the hydrogels show flow-aligning properties. In contrast, Fmoc-K(Boc)LV forms highly branched fibrils that produce isotropic hydrogels with a much higher modulus (G′ > 104 Pa), and lower concentration for hydrogel formation. The distinct self-assembled structures are ascribed to conformational differences, as revealed by secondary structure probes (CD, FTIR, Raman spectroscopy) and X-ray diffraction. Fmoc-VLK(Boc) forms well-defined β-sheets with a cross-β X-ray diffraction pattern, whereas Fmoc-KLV(Boc) forms unoriented assemblies with multiple stacked sheets. Interchange of the K and V residues when inverting the tripeptide sequence thus leads to substantial differences in self-assembled structures, suggesting a promising approach to control hydrogel properties.

Development of Anilino-Maytansinoid ADCs that Efficiently Release Cytotoxic Metabolites in Cancer Cells and Induce High Levels of Bystander Killing

Antibody anilino maytansinoid conjugates (AaMCs) have been prepared in which a maytansinoid bearing an aniline group was linked through the aniline amine to a dipeptide, which in turn was covalently attached to a desired monoclonal antibody. Several such

Engineering Enzyme-Cleavable Oligonucleotides by Automated Solid-Phase Incorporation of Cathepsin B Sensitive Dipeptide Linkers

Oligonucleotides containing cleavable linkers have emerged as versatile tools to achieve stimulus-responsive and site-specific cleavage of DNA. However, the limitations of previously reported cleavable linkers including photolabile and disulfide linkers have restricted their applications in vivo. Inspired by the cathepsin B-sensitive dipeptide linkers in antibody–drug conjugates (ADCs) such as Adcetris, we have developed Val-Ala-02 and Val-Ala-Chalcone phosphoramidites for the automated synthesis of enzyme-cleavable oligonucleotides. Cathepsin B digests Val-Ala-02 and Val-Ala-Chalcone linkers efficiently, enabling cleavage of oligonucleotides into two components or release of small-molecule payloads. Based on the prior success of dipeptide linkers in ADCs, we believe that these dipeptide linker phosphoramidites will promote new clinical applications of therapeutic oligonucleotides.

A Wireframe DNA Cube: Antibody Conjugate for Targeted Delivery of Multiple Copies of Monomethyl Auristatin E

In recent years, several antibody drug conjugates (ADC) have been accepted by the FDA as therapeutics against cancer. It is well-known that control of drug-to-antibody ratio (DAR) is vital for the success of an ADC, which inspires the advancement of bette

ANTIBODY-DRUG CONJUGATE

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Linker, Antibody-Drug Conjugate Including Same and Use Thereof

Provided are a linker represented by Formula I or I′, an antibody-drug conjugate containing the same, and use of thereof, a pharmaceutical composition comprising the antibody-drug conjugate, and use of the antibody-drug conjugate for treating and/or preventing a disease.