1311933-82-0

Basic information

• Product Name: (R)-N-Fmoc-2-(3'-butenyl)alanine
• Synonyms: (R)-N-Fmoc-2-(3'-butenyl)alanine;(R)-2-((((9H-Fluoren-9-yl)Methoxy)carbonyl)aMino)-2-Methylhex-5-enoic acid;FMoc-α-Me-D-Gly(Butenyl)-OH;(2R)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-2-methyl-5-hexenoic acid;(9H-Fluoren-9-yl)MethOxy]Carbonyl Alpha-Methyl-D-Gly(Butenyl)-OH
• CAS NO: 1311933-82-0
• Molecular Formula: C22H23NO4
• Molecular Weight: 365.42232
• EINECS: -0
• Mol File: 1311933-82-0.mol

Chemical Properties

• Boiling Point: 575.6±45.0 °C(Predicted)
• Appearance: /
• Density: 1.203±0.06 g/cm3(Predicted)
• Storage Temp.: Sealed in dry,Room Temperature
• PKA: 3.95±0.11(Predicted)
• CAS DataBase Reference: (R)-N-Fmoc-2-(3'-butenyl)alanine(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-N-Fmoc-2-(3'-butenyl)alanine(1311933-82-0)
• EPA Substance Registry System: (R)-N-Fmoc-2-(3'-butenyl)alanine(1311933-82-0)

Safety Data

• Hazardous Substances Data: 1311933-82-0(Hazardous Substances Data)

Usage

Uses

Used in Organic Chemistry:
(R)-N-Fmoc-2-(3'-butenyl)alanine is used as a building block for the synthesis of peptides and proteins, allowing chemists to incorporate it into specific sequences to confer unique chemical properties or functionalities.
Used in Drug Discovery:
(R)-N-Fmoc-2-(3'-butenyl)alanine is used as a key component in the development of new pharmaceuticals, providing a versatile structure that can be modified to target specific biological pathways or receptors.
Used in Chemical Biology:
(R)-N-Fmoc-2-(3'-butenyl)alanine is utilized as a tool in chemical biology to study the interactions between small molecules and biological systems, potentially leading to the discovery of new bioactive molecules.
Used in Biochemistry:
(R)-N-Fmoc-2-(3'-butenyl)alanine is employed in biochemistry for the investigation of protein structure and function, as well as for the development of novel bioconjugation strategies.

Upstream product

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

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.

Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors

HIV-1 integrase (IN) catalyzes the integration of viral DNA into the host genome, involving several interactions with the viral and cellular proteins. We have previously identified peptide IN inhibitors derived from the α-helical regions along the dimeric interface of HIV-1 IN. Herein, we show that appropriate hydrocarbon stapling of these peptides to stabilize their helical structure remarkably improves the cell permeability, thus allowing inhibition of the HIV-1 replication in cell culture. Furthermore, the stabilized peptides inhibit the interaction of IN with the cellular cofactor LEDGF/p75. Cellular uptake of the stapled peptide was confirmed in four different cell lines using a fluorescein-labeled analogue. Given their enhanced potency and cell permeability, these stapled peptides can serve as not only lead IN inhibitors but also prototypical biochemical probes or nanoneedles for the elucidation of HIV-1 IN dimerization and host cofactor interactions within their native cellular environment.