Fmoc-N-Me-Trp(Boc)-OH (CAS 197632-75-0) belongs to the n-methylated protected amino-acid building block class. It is used in backbone N-methylated peptide and peptidomimetic synthesis, particularly where backbone N-methylation, conformational tuning and proteolytic-stability/SAR studies is required.

N-methylation increases steric demand during coupling; reagent choice and coupling time may need adjustment relative to the unmethylated residue. Procurement should match the exact CAS, protection state and lot-specific analytical specification to the intended route.

Product Information

Backbone N-Methylation

Fmoc-N-Me-Trp(Boc)-OH introduces an N-methylated amino-acid unit into peptide or peptidomimetic synthesis. Backbone N-methylation removes an amide hydrogen after incorporation and can alter local conformation, hydrogen bonding and proteolytic susceptibility.

Coupling Considerations

N-methylated residues are more sterically demanding than their unmethylated analogs. Difficult couplings may require stronger activation, longer reaction time or sequence-specific optimization rather than simple reagent excess.

Selection in SAR Programs

Use the exact residue and stereochemistry required by the design. N-methylation and side-chain changes should be treated as separate variables when interpreting conformational or activity effects.

Compare neighboring reagents in our noncanonical amino acids. Full-sequence work is covered under protected peptide building blocks.

Product Documents

MSDS - Fmoc-N-Me-Trp(Boc)-OH (AS4241)

The Safety Data Sheet provides product identification, hazard information, handling and storage guidance, exposure controls, transport information, and regulatory information for laboratory use.

Certificates of Analysis (COAs) are batch-specific. Please contact us to request the COA for your product, and we will provide it by email.

Frequently Asked Questions

What does N-methylation change in Fmoc-N-Me-Trp(Boc)-OH?

It removes a backbone amide hydrogen after incorporation and can alter local hydrogen bonding, conformation and proteolytic susceptibility.

Can Fmoc-N-Me-Trp(Boc)-OH be more difficult to couple?

Yes. Its N-methylated backbone nitrogen is more sterically demanding than the corresponding unmethylated residue, so activation and reaction time may need sequence-specific adjustment.

Can the opposite stereoisomer replace Fmoc-N-Me-Trp(Boc)-OH?

No. Stereochemistry and N-methylation are independent structural variables and can produce different peptide conformations.

Research Use Only.