150308-80-8

Basic information

• Product Name: N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine
• Synonyms: N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine;Fmoc-Sec(mbzl)-OH;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-3-[[(4-methoxyphenyl)methyl]seleno]-L-alanine;FMoc-(R)-4-Methoxybenzyl selenocysteine;(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-((4-methoxybenzyl)selanyl)propanoic acid;Fmoc-L-Sec(pMeOBzl)-OH;(9H-Fluoren-9-yl)MethOxy]Carbonyl Sec(Mob)-OH
• CAS NO: 150308-80-8
• Molecular Formula: C₂₆H₂₅NO₅Se
• Molecular Weight: 510.44
• Product Categories: amino acid;Seleno Amino Acid;amino acids
• Mol File: 150308-80-8.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 708.5±60.0 °C(Predicted)
• Appearance: /
• Storage Temp.: Store at +2°C to +8°C.
• PKA: 3.50±0.10(Predicted)
• CAS DataBase Reference: N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine(CAS DataBase Reference)
• NIST Chemistry Reference: N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine(150308-80-8)
• EPA Substance Registry System: N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine(150308-80-8)

Safety Data

• Hazardous Substances Data: 150308-80-8(Hazardous Substances Data)

Usage

Description

N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine is a specialized amino acid derivative used as a building block in the field of peptide synthesis. It is designed for the introduction of selenocysteine during Fmoc solid-phase peptide synthesis (SPPS) and is crucial for the development of peptides with specific biological activities. N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine is a white or off-white powder and is stable to trifluoroacetic acid (TFA), making it suitable for various peptide synthesis applications.

Uses

Used in Pharmaceutical Industry:
N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine is used as a key building block for the synthesis of seleno-peptides, which have potential applications in drug development. These seleno-peptides can exhibit unique biological activities and properties, making them valuable for the creation of novel therapeutic agents.
Used in Research and Development:
In the research and development sector, N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine is utilized for the synthesis of peptides containing selenocysteine residues. These peptides can be employed in various biological studies, including investigations into the mechanisms of selenium's role in health and disease, as well as the development of new diagnostic tools and therapeutic strategies.
Used in Peptide Synthesis:
N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine is used as an essential component in the solid-phase peptide synthesis (SPPS) process. It allows for the incorporation of selenocysteine into the peptide chain, which can lead to the formation of peptides with enhanced stability and biological activity. The compound's stability to TFA makes it suitable for use in various peptide synthesis protocols.
Used in the Synthesis of Selenoproteins:
N-9-fluorenylmethoxycarbonyl-Se-4-methoxybenzylselenocysteine is used in the synthesis of selenoproteins, which are proteins containing selenocysteine residues. These selenoproteins play crucial roles in various biological processes, including antioxidant defense, thyroid hormone metabolism, and immune function. The compound facilitates the production of these proteins for research and potential therapeutic applications.

Upstream product

• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 146552-76-3 Se-(4-methoxybenzyl)-L-selenocysteine 
• 342904-13-6 Fmoc-(Se)-p-methoxybenzylselenocysteine-OAll 
• 62212-22-0 1,2-bis(4-methoxybenzyl)diselane 
• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 136497-85-3 N-(9-fluorenylmethoxycarbonyl)-L-serine allyl ester 
• 824-94-2 p-methoxybenzyl chloride 
• 847354-75-0 (4-methoxy-phenyl)-methaneselenol 
• 342904-04-5 Fmoc-(OTs)-serine-OAll 
• 1365284-58-7 Fmoc-Sec(Mob)-OMe 
• 82911-78-2 N-[(9-fluorenylmethoxy)carbonyl]-L-serine methyl ester 
• 229962-91-8 methyl (2S)-2-(((9H-fluoren-9-ylmethoxy)carbonyl)amino)-3-(((4-methylbenzene)sulfonyl)oxy)propanoate 
• 105-13-5 4-Methoxybenzyl alcohol 
• 1246371-30-1 L-selenocystine 

Downstream Products

• 959415-37-3 1-diazo-3-({[(9H-fluoren-9-yl)methoxy]carbonyl}amino)-4-[(4-methoxybenzyl)selanyl]butan-2-one 
• 1421916-70-2 H-MEELYKSG(¹³C-1)U-NH₂ 
• 1421916-71-3 H-MEELYKSG(¹³C-1)U-OH 
• 1421916-65-5 H-DTHFPICIFCCGU-NH₂ 
• 1421916-80-4 H-C(5-NPys)RKFFARIRGGRGU(5-Npys)-NH₂ 

Relevant articles and documents

Improved synthetic routes to the selenocysteine derivatives useful for Boc-based peptide synthesis with benzylic protection on the selenium atom

Selenocysteine (Sec) derivatives, i.e., Boc-Sec(MBn)-OH (1) and Boc-Sec(MPM)-OH (2), which are useful for chemical synthesis of selenopeptides, were obtained from L-serine in five steps with total yields of 73% and 74%, respectively. The enantiomeric excesses were confirmed to be >99% e.e. by optical resolution using a chiral column on HPLC. On the other hand, for the case of a Fmoc-protected Sec derivative, i.e., Fmoc-Sec(MPM)-OH, similar reactions resulted in low yields and partial racemization taking place. [PRESENTED EQUATION]

Investigation of peptide thioester formation via N→Se acyl transfer

Native chemical ligation is widely used for the convergent synthesis of proteins. The peptide thioesters required for this process can be challenging to produce, particularly when using Fmoc-based solid-phase peptide synthesis. We have previously reported a route to peptide thioesters, following Fmoc solid-phase peptide synthesis, via an N→S acyl shift that is initiated by the presence of a C-terminal cysteine residue, under mildly acidic conditions. Under typical reaction conditions, we occasionally observed significant thioester hydrolysis as a consequence of long reaction times (~48h) and sought to accelerate the reaction. Here, we present a faster route to peptide thioesters, by replacing the C-terminal cysteine residue with selenocysteine and initiating thioester formation via an N→Se acyl shift. This modification allows thioester formation to take place at lower temperatures and on shorter time scales. We also demonstrate how application of this strategy also accelerates peptide cyclization, when a linear precursor is furnished with an N-terminal cysteine and C-terminal selenocysteine.

Preparation of the β3-homoselenocysteine derivatives Fmoc-β3hSec(PMB)-OH and Boc-β3hSec(PMB)-OH for solution and solid-phase-peptide synthesis and selenoligation

The title compounds, 4 and 7, have been prepared from the corresponding α-amino acid derivative selenocystine (1) by the following sequence of steps: cleavage of the Se-Se bond with NaBH4, p-methoxybenzyl (PMB) protection of the SeH group, Fmoc or Boc protection at the N-atom and Arndt-Eistert homologation (Schemes 1 and 2). A β3-heptapeptide 8 with an N-terminal β3-hSec(PMB) residue was synthesized on Rink amide AM resin and deprotected ('in air') to give the corresponding diselenide 9, which, in turn, was coupled with a β3-tetrapeptide thiol ester 10 by a seleno-ligation. The product β3- undecapeptide was identified as its diselenide and its mixed selenosulfide with thiophenol (Scheme 3). The differences between α- and β-Sec derivatives are discussed.