1093645-21-6

Basic information

• Product Name: (R)-N-Fmoc-2-(4'-pentenyl)glycine
• Synonyms: (R)-N-Fmoc-2-(4'-pentenyl)glycine;(2R)-2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-6-heptenoic acid;(R)-2-((((9H-Fluoren-9-yl)Methoxy)carbonyl)aMino)hept-6-enoic acid;(2R)-2-(Fmoc-amino)-6-heptenoic acid
• CAS NO: 1093645-21-6
• Molecular Formula: C22H23NO4
• Molecular Weight: 365
• EINECS: -0
• Mol File: 1093645-21-6.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 589.7±45.0 °C(Predicted)
• Appearance: /
• Density: 1.202
• Storage Temp.: 2-8°C
• PKA: 3.87±0.21(Predicted)
• CAS DataBase Reference: (R)-N-Fmoc-2-(4'-pentenyl)glycine(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-N-Fmoc-2-(4'-pentenyl)glycine(1093645-21-6)
• EPA Substance Registry System: (R)-N-Fmoc-2-(4'-pentenyl)glycine(1093645-21-6)

Safety Data

• Hazardous Substances Data: 1093645-21-6(Hazardous Substances Data)

Usage

General Description

(R)-N-Fmoc-2-(4'-pentenyl)glycine is a chemical compound commonly used in the field of organic chemistry. It is a derivative of the amino acid glycine, with an added Fmoc protecting group and a 4'-pentenyl substituent. The Fmoc group is often utilized to protect the amine group of the glycine, while the 4'-pentenyl substituent introduces a double bond into the molecule, adding functional groups that can be further modified through chemical reactions. (R)-N-Fmoc-2-(4'-pentenyl)glycine is frequently employed in the synthesis of peptides and other bioactive molecules, as well as in the study of protein structure and function. Additionally, its unique structure makes it a valuable building block for the creation of new drug candidates and other biologically active compounds.

Upstream product

• 1093645-18-1 C₂₃H₂₅NO₄ 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 1119-51-3 bromopentene 

Relevant articles and documents

Switching substitution groups on the in-tether chiral centre influences backbone peptides' permeability and target binding affinity

Different substitution groups on the in-tether chiral centre of chirality-induced helical peptides (CIH peptides) showed distinguishable effects on the peptides' cellular uptakes and binding affinities with the estrogen receptor α(ER-α). This study proves that in-tether chiral centres are a valuable modification site for constructing peptide ligands with preferable biophysical properties.

Novel potent apoA-I peptide mimetics that stimulate cholesterol efflux and pre-β particle formation in vitro

Reverse cholesterol transport (RCT) is believed to be the primary mechanism by which HDL and its major protein apoA-I protect against atherosclerosis. Starting from the inactive 22-amino acid peptide representing the consensus sequence of the class A amphipathic helical repeats of apoA-I, we designed novel peptides able to mobilize cholesterol from macrophages in vitro, and to stimulate the formation of 'nascent HDL' particles, with potency comparable to the entire apoA-I protein.