1418181-50-6

Basic information

• Product Name: (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropanethioic S-acid
• Synonyms: (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropanethioic S-acid
• CAS NO: 1418181-50-6
• Molecular Weight: 403.502
• Mol File: 1418181-50-6.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropanethioic S-acid(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropanethioic S-acid(1418181-50-6)
• EPA Substance Registry System: (S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropanethioic S-acid(1418181-50-6)

Safety Data

• Hazardous Substances Data: 1418181-50-6(Hazardous Substances Data)

Upstream product

• 35661-40-6 N-Fmoc L-Phe 
• 101214-43-1 Fmoc-Phe-ONSu 
• 860800-19-7 9H-fluoren-9-ylmethyl N-[(1S)-1-benzyl-2-benzotriazol-1-yl-2-oxoethyl]carbamate 

Downstream Products

• 1429502-18-0 C₄₃H₄₁N₃O₆ 

Relevant articles and documents

Electrophilic Sulfonium-Promoted Peptide and Protein Amidation in Aqueous Media

A novel amidation strategy using electrophilic sulfonium, which is soluble and stable in aqueous conditions, was developed. The sulfoniums could activate thioacid and carboxyl acid to efficiently react with amines to afford amides. This method enables applications in amidation in both aqueous media and solid-phase peptide synthesis, peptide/protein modifications, and reactive lysines of a proteome at pH 10 with activity-based protein profiling. A peptide ligand-directed labeling of the USP7-UBL2 domain was also performed using this method.

Site-Specific Incorporation of Multiple Thioamide Substitutions into a Peptide Backbone via Solid Phase Peptide Synthesis

Among various peptide modification strategies, thioamide substitution by replacing the carbonyl oxygen atom of an amide bond with a sulfur atom constitutes an invaluable tool for chemical biology, for use in peptide drug discovery and protein structure-fu

Ynamide-Mediated Thiopeptide Synthesis

Exploration of the full potential of thioamide substitution as a tool in the chemical biology of peptides and proteins has been hampered by insufficient synthetic strategies for the site-specific introduction of a thioamide bond into a peptide backbone. A novel ynamide-mediated two-step strategy for thiopeptide bond formation with readily available monothiocarboxylic acids as thioacyl donors is described. The α-thioacyloxyenamide intermediates formed from the ynamides and monothiocarboxylic acids can be purified, characterized, and stored. The balance between their activity and stability enables them to act as effective thioacylating reagents to afford thiopeptide bonds under mild reaction conditions. Amino acid functional groups such as OH, CONH2, and indole NH groups need not be protected during thiopeptide synthesis. The modular nature of this strategy enables the site-specific incorporation of a thioamide bond into peptide backbones in both solution and the solid phase.