288617-74-3

Basic information

• Product Name: (S)-N-FMoc-2-(5'-pentenyl)alanine
• Synonyms: (S)-N-FMoc-2-(5'-pentenyl)alanine;(S)-2-((((9H-Fluoren-9-yl)Methoxy)carbonyl)aMino)-2-Methyloct-7-enoic acid;(S)-N-FMoc-2-(5'-hexenyl)alanine;FMoc-α-Me-Gly(Hexenyl)-OH;(S)-N-Fmoc-2-(5'-hexyl)alanine;(9H-Fluoren-9-yl)MethOxy]Carbonyl Alpha-Methyl-Gly(Hexenyl)-OH
• CAS NO: 288617-74-3
• Molecular Formula: C24H27NO4
• Molecular Weight: 393.47548
• Mol File: 288617-74-3.mol
• Article Data: 2

Chemical Properties

• Boiling Point: 605.3±55.0 °C(Predicted)
• Appearance: /
• Density: 1.169±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 3.94±0.41(Predicted)
• CAS DataBase Reference: (S)-N-FMoc-2-(5'-pentenyl)alanine(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-N-FMoc-2-(5'-pentenyl)alanine(288617-74-3)
• EPA Substance Registry System: (S)-N-FMoc-2-(5'-pentenyl)alanine(288617-74-3)

Safety Data

• Hazardous Substances Data: 288617-74-3(Hazardous Substances Data)

Usage

General Description

"(S)-N-FMoc-2-(5'-pentenyl)alanine is a specific type of amino acid derivative used prominently within the realm of organic and medicinal chemistry. As an Fmoc (9-fluorenylmethyloxycarbonyl) protected amino acid, its main use is during the process of solid-phase peptide synthesis. The Fmoc component plays a crucial role as a protective group for an amino acid's amine functionality, preventing potential side reactions from occurring during the peptide synthesis. The pentenyl side chain of this chemical can potentially be utilized for further chemical modifications, giving it significant relevance in drug development and study. Overall, (S)-N-FMoc-2-(5'-pentenyl)alanine is an important amino acid derivative with significant uses in the development and synthesis of peptides.

Upstream product

• 1445137-81-4 (S)-2-(benzyloxycarbonylamino)-2-methyloct-7-enoic acid 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 18922-04-8 6-iodohex-1-ene 
• 84418-43-9 9-fluorenylmethyl carbamate 

Downstream Products

• 1445137-70-1 C₈₀H₁₂₂N₁₈O₁₄ 

Relevant articles and documents

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.