Fmoc-Met(O2)-OH

Fmoc-Met(O2)-OH is a specialized Fmoc-protected amino acid building block designed for the incorporation of methionine sulfone residues into peptide sequences via Fmoc SPPS. The methionine sulfone residue introduced by Fmoc-Met(O2)-OH exhibits significantly enhanced oxidative stability compared to native methionine, as the sulfur is already in its fully oxidized state and cannot undergo further oxidation to methionine sulfoxide or sulfone during peptide synthesis, purification, or storage. This makes Fmoc-Met(O2)-OH particularly valuable for the synthesis of peptides intended for long-term storage or for studies involving oxidative stress and protein folding. The Fmoc protecting group of Fmoc-Met(O2)-OH enables efficient incorporation into growing peptide chains under standard SPPS conditions, with selective deprotection achieved using piperidine without affecting the sulfone moiety. For researchers requiring peptides with methionine residues that cannot be oxidized during handling or biological assays, Fmoc-Met(O2)-OH provides a definitive solution.

Product Parameters

Why Cosperpharm?

When your peptide synthesis campaign demands building blocks that deliver consistent quality and batch-to-batch reproducibility, Cosperpharm provides Fmoc-Met(O2)-OH with the analytical rigor and supply reliability that pharmaceutical and biotech customers require.

Oxidation state matters. Methionine sulfone residues introduced via Fmoc-Met(O2)-OH are fully oxidized and cannot degrade further—meaning your final peptide's oxidative stability is locked in from the start. Any impurity or isomer in this building block will compromise your peptide's purity and biological activity. Our analytical release protocol includes HPLC purity verification (≥98%), optical rotation confirmation, identity testing (IR), and moisture determination—because peptide quality begins with the building block.

Documentation that supports regulatory submission. Every shipment includes a Certificate of Analysis (COA) with batch-specific HPLC purity, optical rotation data, and chromatographic traceability. Custom quality agreements and additional documentation packages are available upon request for customers preparing regulatory submissions.

Flexible supply across all development stages. Cosperpharm supplies Fmoc-Met(O2)-OH from 1g–50g for research and method development, to 100g–500g for process validation, to kilogram-scale for commercial peptide manufacturing. R&D samples ship within 5–7 business days; bulk orders ship within 2–3 weeks.

Technical support from peptide chemists. Our team has extensive experience with Fmoc SPPS and can advise on coupling conditions, deprotection protocols, and compatibility with various resin systems for methionine sulfone-containing peptides.

Global reach with transparent pricing. Cosperpharm ships to pharmaceutical manufacturers, CROs, and research institutions worldwide, with full customs documentation included. Volume discounts apply at larger scales.

Product Advantages

 Fully Oxidized, Redox-Stable Methionine Surrogate

Fmoc-Met(O2)-OH introduces methionine sulfone—the fully oxidized form of methionine—into peptide sequences. Unlike native methionine, which is susceptible to oxidation during synthesis, purification, storage, and biological assays, the sulfone moiety is chemically inert and cannot undergo further oxidation. This eliminates a major source of peptide heterogeneity and degradation.

 Standard Fmoc SPPS Building Block

Fmoc-Met(O2)-OH is fully compatible with standard Fmoc solid-phase peptide synthesis protocols. The Fmoc group enables selective deprotection with piperidine, while the sulfone side chain remains unaffected under standard coupling, deprotection, and cleavage conditions. This allows seamless incorporation into any Fmoc-based peptide synthesis workflow without requiring protocol modifications.

 Enables Study of Oxidative Stress and Protein Folding

The methionine sulfone residue introduced by Fmoc-Met(O2)-OH serves as a valuable tool in studying oxidative stress, protein folding, and the biological roles of methionine oxidation. Researchers can use methionine sulfone-containing peptides as stable analogs to investigate the effects of methionine oxidation on protein structure and function.

 High Purity with Full Characterization

Cosperpharm supplies Fmoc-Met(O2)-OH with ≥98% HPLC purity, confirmed optical rotation, and full analytical characterization including IR identity testing. Each batch is released with a comprehensive COA ensuring batch-to-batch consistency for reproducible peptide synthesis.

FAQ

Q1: What is the difference between Fmoc-Met(O2)-OH and Fmoc-Met(O)-OH?

A: Fmoc-Met(O2)-OH is the sulfone form of methionine (sulfur oxidation state +4), whereas Fmoc-Met(O)-OH is the sulfoxide form (oxidation state +2). The sulfone is fully oxidized and cannot undergo further oxidation, making it more stable than the sulfoxide.

Q2: What is the primary application of Fmoc-Met(O2)-OH?

A: Fmoc-Met(O2)-OH is used as a standard building block for the introduction of methionine sulfone residues into peptides via Fmoc solid-phase peptide synthesis (SPPS). It is particularly useful when oxidative stability of the methionine residue is required.

Contact Us

Need Fmoc-Met(O2)-OH for your next peptide synthesis project? Cosperpharm makes sourcing high-quality Fmoc amino acids straightforward. Contact our team today for pricing, availability, or technical support—we're here to help you succeed.