288617-78-7

Basic information

• Product Name: (R)-N-FMoc-2-(5'-pentenyl)alanine
• Synonyms: (R)-N-FMoc-2-(5'-pentenyl)alanine;(R)-N-FMoc-2-(5'-hexenyl)alanine;FMoc-α-Me-D-Gly(Hexenyl)-OH;(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-2-methyloct-7-enoic acid;(R)-N-Fmoc-2-(5'-hexyl)alanine;(9H-Fluoren-9-yl)MethOxy]Carbonyl Alpha-Methyl-D-Gly(Hexenyl)-OH
• CAS NO: 288617-78-7
• Molecular Formula: C24H27NO4
• Molecular Weight: 393.47548
• Mol File: 288617-78-7.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: (R)-N-FMoc-2-(5'-pentenyl)alanine(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-N-FMoc-2-(5'-pentenyl)alanine(288617-78-7)
• EPA Substance Registry System: (R)-N-FMoc-2-(5'-pentenyl)alanine(288617-78-7)

Safety Data

• Hazardous Substances Data: 288617-78-7(Hazardous Substances Data)

Usage

General Description

The chemical (R)-N-FMoc-2-(5'-pentenyl)alanine is a derivative of the amino acid alanine, with an added 5'-pentenyl group and a FMoc (9-fluorenylmethoxycarbonyl) protecting group. (R)-N-FMoc-2-(5'-pentenyl)alanine is commonly used in peptide synthesis as a building block for creating custom peptides with specific functional groups. The (R) configuration of the molecule indicates that it has a specific chirality, which can be important in the context of protein interactions and activity. This chemical is used in the fields of biochemistry and drug development for its ability to modify and manipulate peptides for various research and therapeutic applications.

Upstream product

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