$246.00 - $1231.00
Fmoc-D-Met-OH is an Fmoc-protected D-methionine building block used to introduce D-Met during Fmoc solid-phase peptide synthesis. The methionine thioether normally remains unprotected during synthesis, so no additional side-chain protecting group is required.
A key handling and QC consideration is methionine oxidation. Oxidation of the thioether to methionine sulfoxide adds one oxygen atom and produces an approximately +16 Da mass shift. For oxidation-sensitive projects, lot condition, solution exposure and analytical evidence for oxidized species may be more important than for non-sulfur hydrophobic amino acids.
Product Information
| Product Name | Fmoc-D-Met-OH |
| Catalog No. | AS3026 |
| CAS No. | 112883-40-6 |
| Molecular Formula | C20H21NO4S |
| Molecular Weight | 371.45 g/mol |
| Protecting Groups | Fmoc alpha-amino protection; methionine thioether unprotected |
| Primary Application | D-methionine incorporation in Fmoc-SPPS |
Application Scope and Assay Relevance
Primary use: Building block for D-methionine incorporation in peptide analogs; the sulfur-containing side chain remains oxidation-sensitive even though the residue is D-configured.
| Typical in vitro relevance | D-Met occurs in bioactive peptide motifs such as dermenkephalin and in synthetic formyl-peptide-receptor ligands. Relevant downstream assays include receptor binding, calcium-mobilization or other cell-signaling assays, protease stability and oxidation-state analysis by LC-MS. |
| In vivo relevance | Final D-Met-containing peptides may be used in animal studies when target activity is retained. D-configuration can change protease recognition, but methionine oxidation must still be controlled. |
Methionine oxidation is a practical QC variable
The Met thioether can oxidize to sulfoxide during storage or handling. This creates a chemically distinct impurity with an approximately +16 Da mass shift.
Purchasing and QC Considerations
Review CAS identity, chiral purity and lot-specific chemical purity. Where oxidation matters, examine the COA or analytical data for oxidized species rather than assuming total HPLC purity fully describes the sulfur-oxidation state.
Frequently Asked Questions
Does D-Met need side-chain protection?
The methionine thioether is normally left unprotected in standard Fmoc-SPPS.
What mass change occurs on methionine oxidation?
Formation of methionine sulfoxide adds approximately +16 Da.
Why monitor oxidation?
Oxidized Met can change the chemical composition and behavior of the building block or final peptide.
Product Documents
A Material Safety Data Sheet (MSDS) is available for this product to support laboratory handling, storage and safety assessment.
Certificates of Analysis (COAs) are batch-specific. Please contact us to request the COA for your product, and we will provide it by email.
Related Technical Resources
See Chemical Peptide Synthesis for a closely related building block or synthesis resource.
Browse the complete D-Form Amino Acids category or use Alan Scientific's Chemical Peptide Synthesis service for custom peptides containing D-amino acids.