288617-72-1

Basic information

• Product Name: (S)-N-Fmoc-2-(3'-butenyl)alanine
• Synonyms: (S)-N-Fmoc-2-(3'-butenyl)alanine;(2S)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-2-methyl-5-hexenoic acid;(S)-2-((((9H-Fluoren-9-yl)Methoxy)carbonyl)aMino)-2-Methylhex-5-enoic acid;FMoc-α-Me-Gly(Butenyl)-OH;(9H-Fluoren-9-yl)MethOxy]Carbonyl Alpha-Methyl-Gly(Butenyl)-OH
• CAS NO: 288617-72-1
• Molecular Formula: C22H23NO4
• Molecular Weight: 365
• EINECS: -0
• Mol File: 288617-72-1.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: (S)-N-Fmoc-2-(3'-butenyl)alanine(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-N-Fmoc-2-(3'-butenyl)alanine(288617-72-1)
• EPA Substance Registry System: (S)-N-Fmoc-2-(3'-butenyl)alanine(288617-72-1)

Safety Data

• Hazardous Substances Data: 288617-72-1(Hazardous Substances Data)

Usage

General Description

"(S)-N-Fmoc-2-(3'-butenyl)alanine is a chemical compound used in the field of chemistry, specifically in peptide synthesis, considering this can be used as a building block for peptides. Its IUPAC name is (S)-2-(((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-butenyl-3-butenoic acid. The compound, categorized as an unusual amino acid, is an N-Fmoc protected form of a (S)-2-(3'-butenyl)alanine, where Fmoc stands for fluorenylmethyloxycarbonyl, a base-sensitive protective group. Its specific structure, with a butenyl side chain, makes it unique and potentially allows for interesting interactions in synthesized proteins. It is often used in laboratories and is not typically found in nature.

Upstream product

• 84418-43-9 9-fluorenylmethyl carbamate 
• 1011309-60-6 C₇H₁₃NO₂ 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 1445137-80-3 (S)-2-(benzyloxycarbonylamino)-2-methylbut-4-enoic acid 

Downstream Products

• 1445137-68-7 C₇₆H₁₁₄N₁₈O₁₄ 

Relevant articles and documents

Influence of α-methylation in constructing stapled peptides with olefin metathesis

Ring-closing metathesis is commonly utilized in peptide macro-cyclization. The influence of α-methylation of the amino acids bearing the olefin moieties has never been systematically studied. In this report, controlled reactions unambiguously indicate that α-methylation at the N-terminus of the metathesis sites is crucial for this reaction to occur. Also, we first elucidated that the E-isomers of stapled peptides are significantly more helical than the Z-isomers.

An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides [8]

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