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Usage

Uses

Used in Peptide Synthesis:
FMoc-N-Me-Cys(Trt)-OH is used as a building block for the synthesis of peptides or peptide fragments. Its Fmoc protection allows for selective deprotection and coupling during solid-phase peptide synthesis, enabling the stepwise assembly of complex peptide structures.
Used in Peptide Thioester Preparation:
FMoc-N-Me-Cys(Trt)-OH is used as a building block to prepare peptide thioesters under acidic conditions. The residue attached to the amino group of N-methylcysteine can migrate to the cysteinyl thiol group, resulting in the formation of a peptide thioester. This process is facilitated by the use of HATU as a coupling reagent in the presence of DIPEA (N,N-Diisopropylethylamine).
Used in Solid-Phase Synthesis of Triostin A:
FMoc-N-Me-Cys(Trt)-OH is used in the solid-phase synthesis of Triostin A, a peptide natural product with potential therapeutic applications. FMoc-N-Me-Cys(Trt)-OH serves as a key intermediate in the assembly of the dithiol Triostin A structure.
Used in the Preparation of Fmoc-N-Me-Cys(Trt)-OAllyl Intermediate:
FMoc-N-Me-Cys(Trt)-OH can be used to prepare the Fmoc-N-Me-Cys(Trt)-OAllyl intermediate, which is another key building block in the solid-phase synthesis of dithiol Triostin A. This intermediate allows for further functionalization and modification of the peptide structure during synthesis.

Upstream product

• 166169-98-8 N-methyl-Cys(Trt) 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 2799-07-7 S-trityl-L-cysteine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 

Relevant academic research and scientific papers

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.

Solid-Phase Synthesis of Triostin A Using a Symmetrical Bis(diphenylmethyl) Linker System

Triostin A is a symmetric bicyclic depsipeptide with very potent antitumoral activity because of its bisintercalation into DNA. In this study, we report a new synthetic strategy that exploits a structural symmetry of triostin A. First, we prepared a novel symmetric linker molecule that is labile under mildly acidic conditions and suitable for a solid-phase synthesis procedure. Two Cys units were attached to a linker-resin conjugate via their free thiol groups, and double deprotection and double coupling reactions were then applied to synthesize linear tetradepsipeptides. Subsequently, the key biscyclization of the tetradepsipeptides was performed on the resin, and the resulting cyclic octapeptide was detached from the linker-resin conjugate to give a peptide with two free thiols. Finally, triostin A was obtained by oxidizing the free thiols in solution to produce a disulfide. The yield was improved through exploration of two different solid-phase synthetic approaches under similar strategy. Mainly, this strategy was developed to enable the ease and rapid preparation of libraries of symmetric bicyclic depsipeptides. It also addresses several synthetic problems with our synthesis, including diketopiperazine (DKP) formation, poor cyclization yields and preparation of noncommercial N-methyl amino acids in good yields.

N-Alkyl cysteine-assisted thioesterification of peptides

A new method for the preparation of peptide thioester by the post-solid phase peptide synthesis (SPPS) approach was developed. A series of N-alkyl cysteine derivatives were prepared and used as the C-terminus residue of the peptides prepared by the Fmoc S