1207188-92-8

Basic information

• Product Name: N-(9-fluorenylmethoxycarbonyl)-L-leucyl-N-ethyl-S-triphenylmethyl-L-cysteine
• Synonyms: N-(9-fluorenylmethoxycarbonyl)-L-leucyl-N-ethyl-S-triphenylmethyl-L-cysteine
• CAS NO: 1207188-92-8
• Molecular Weight: 726.937
• Mol File: 1207188-92-8.mol

Chemical Properties

• CAS DataBase Reference: N-(9-fluorenylmethoxycarbonyl)-L-leucyl-N-ethyl-S-triphenylmethyl-L-cysteine(CAS DataBase Reference)
• NIST Chemistry Reference: N-(9-fluorenylmethoxycarbonyl)-L-leucyl-N-ethyl-S-triphenylmethyl-L-cysteine(1207188-92-8)
• EPA Substance Registry System: N-(9-fluorenylmethoxycarbonyl)-L-leucyl-N-ethyl-S-triphenylmethyl-L-cysteine(1207188-92-8)

Safety Data

• Hazardous Substances Data: 1207188-92-8(Hazardous Substances Data)

Upstream product

• 86060-88-0 N-(9-fluorenylmethoxycarbonyl)-L-leucine pentafluorophenyl ester 
• 130858-94-5 Fmoc-L-fluoride 
• 1207188-85-9 N-(9-fluorenymethoxycarbonyl)-L-leucyl-N-ethyl-S-triphenylmethyl-L-cysteine allyl ester 

Downstream Products

• 1319726-66-3 Fmoc-Leu-(Et)Cys(Trt)-OBt 

Relevant articles and documents

Efficient preparation of Fmoc-aminoacyl-N-ethylcysteine unit, a key device for the synthesis of peptide thioesters

The synthesis of Fmoc-aminoacyl-N-ethyl-S-triphenylmethylcysteine, an N- to S-acyl migratory device for the preparation of peptide thioesters by Fmoc-SPPS (solid-phase peptide synthesis) is described. Condensation of Fmoc-aminoacyl pentafluorophenyl ester and N-ethyl-S-triphenylmethylcysteine was efficiently performed in the presence of HOOBt (3-hydroxy-3,4-dihydro-4-oxo-1,2,3- benzotriazine) in DMF. A small amount of diastereomer yielded during the reaction was easily separated by HPLC purification and the highly pure devices were obtained for most of the proteinogenic amino acids.

High-pressure-promoted Fmoc-aminoacylation of N-ethylcysteine: preparation of key devices for the solid-phase synthesis of peptide thioesters

In this study synthesis of Fmoc-aminoacyl-N-ethyl-S-triphenylmethylcysteine, a new N→S acyl migratory device for the preparation of peptide thioesters by Fmoc solid-phase peptide synthesis (SPPS) is described. Condensation of Fmoc-aminoacyl fluoride and N-ethyl-S-triphenylmethylcysteine allyl ester, readily prepared from known S-triphenylmethylcysteine allyl ester, was efficiently promoted in CH2Cl2 under high-pressure (800 MPa). When the reaction was performed with the additive DIEA, considerable epimerization at the chiral centers occurred, affording a mixture of diastereomers. When the preparation procedure for N-ethyl-S-triphenylmethylcysteine allyl ester was changed and the additive DIEA in the high-pressure reaction was excluded, Fmoc-aminoacyl-N-ethyl-S-triphenylmethylcysteines was obtained as a single stereoisomer without epimerization. The Fmoc-l-leucine adduct thus prepared was deallylated and used for the SPPS of a known decapeptide. A remarkable increase (44%) in the overall yield of the decapeptidethioester was achieved, compared to the 7% obtained by the stepwise on-resin Leu-Cys condensation method.