Fmoc-N-Methyl-L-Val-OH

Fmoc-N-Methyl-L-Val-OH is an essential building block for the Fmoc SPPS methodology, enabling researchers to generate peptides with predetermined N-methylated amino acid sequences. The strategic incorporation of Fmoc-N-Methyl-L-Val-OH allows scientists to study the impact of this common post-translational modification on protein-protein interactions. When using Fmoc-N-Methyl-L-Val-OH, the N-methylation of valine enhances the compound‘s hydrophobic character and provides rigidity, directly influencing peptide folding dynamics and stability. Furthermore, Fmoc-N-Methyl-L-Val-OH is utilized not only in peptide synthesis but also in various biological applications as enzyme substrates, culture media additives, and research reagents in biochemistry.

Product Parameters

Why Cosperpharm?

When your peptide synthesis campaign requires precision at the backbone level, Cosperpharm supplies Fmoc-N-Methyl-L-Val-OH with the consistency and purity that modern drug discovery demands.

Purity you can depend on for reproducibility. The methylation of the valine amide can sometimes lead to residual byproducts if not carefully controlled. Our Fmoc-N-Methyl-L-Val-OH undergoes rigorous HPLC testing to ensure ≥98% purity, guaranteeing that your peptide assembly proceeds without premature chain termination or sequence deletion. Batch-specific HPLC chromatograms are available upon request.

Supports complex medicinal chemistry workflows. From building N-methylated peptide libraries for hit identification to constructing stabilized lead compounds, our Fmoc-N-Methyl-L-Val-OH integrates seamlessly into standard automated synthesizers. Our technical team can advise on optimized coupling protocols for this sterically hindered tertiary amine, helping you achieve high coupling efficiencies even in difficult sequences.

Documentation for regulatory and R&D needs. Cosperpharm provides full Certificates of Analysis (COA) with each shipment, including optical rotation data to confirm stereochemical integrity and water content analysis to ensure long-term stability. For customers scaling to preclinical studies, we offer custom quality agreements and enhanced characterization packages.

Flexible supply for all scales. Whether you need 1g for exploratory peptide library synthesis or 1kg for process development, Cosperpharm delivers Fmoc-N-Methyl-L-Val-OH with transparent lead times. R&D samples ship within 5–7 business days; bulk orders ship within 2–3 weeks.

Product Advantages

The N-methylation of the valine residue locks the amide bond into a specific conformation, restricting the flexibility of the peptide backbone. When incorporated into peptide sequences, Fmoc-N-Methyl-L-Val-OH forces a turn or kink in the chain, which is essential for designing bioactive peptides with precise three-dimensional structures that mimic native protein binding epitopes.

2. Enhanced Metabolic Stability

N-methylated peptides are significantly more resistant to proteolytic degradation by peptidases than their non-methylated counterparts. By using Fmoc-N-Methyl-L-Val-OH, researchers can generate peptide therapeutics with prolonged plasma half-life and improved oral bioavailability—a proven strategy in drug development.

3. Orthogonal Fmoc Protection Strategy

The Fmoc protecting group on Fmoc-N-Methyl-L-Val-OH is selectively removed under standard piperidine conditions (20% in DMF), orthogonal to acid-labile protecting groups such as Boc and Trt. This allows seamless integration into standard Fmoc SPPS workflows without requiring specialized instrumentation or modified deprotection protocols.

4. Versatile Research Applications

Beyond peptide synthesis, Fmoc-N-Methyl-L-Val-OH serves as an enzyme substrate, culture media additive, and general biochemical reagent. Its applications span from basic research into protein folding dynamics to high-throughput screening of N-methylated peptide libraries.

5. Superior Hydrophobic Character

The methyl group on the nitrogen atom enhances the overall hydrophobicity of the valine side chain environment. This increased hydrophobicity can modulate peptide solubility and membrane permeability, offering additional levers for optimizing physicochemical properties of peptide drug candidates.

Synthetic Route

The preparation of Fmoc-N-Methyl-L-Val-OH typically proceeds through N-methylation of L-valine followed by Fmoc protection of the α-amine. A representative laboratory-scale synthesis described by ChemicalBook involves the following approach:

Step 1 — Preparation of N-methyl-L-valine:

L-Valine is subjected to reductive methylation using formaldehyde and a reducing agent such as sodium cyanoborohydride or via catalytic hydrogenation over palladium. The reaction selectively methylates the α-amino group to yield N-methyl-L-valine.

Step 2 — Fmoc protection:

The N-methyl-L-valine is dissolved in a suitable solvent system (e.g., aqueous dioxane or DMF) containing a base such as sodium carbonate or triethylamine. 9-Fluorenylmethyl chloroformate (Fmoc-Cl) is added dropwise at 0–5 °C, and the mixture is stirred until the reaction is complete (24–72 hours). The reaction mixture is then concentrated and partitioned between ethyl ether and 5% sodium bicarbonate solution. The combined aqueous phase is acidified to pH=2 with 5M hydrochloric acid and extracted with ethyl acetate. The organic extracts are dried, concentrated, and purified to afford Fmoc-N-Methyl-L-Val-OH.

Step 3 — Recrystallization:

The crude product is recrystallized from an appropriate solvent system (e.g., ethyl acetate/hexane) to obtain the final product as a white to off-white crystalline powder.

Contact Us

Starting your next peptide discovery project should be simple and efficient. Reach out to Cosperpharm today to secure high-purity Fmoc-N-Methyl-L-Val-OH for your research needs.