167275-47-0

Basic information

• Product Name: FMoc-α-Me-Pro-OH
• Synonyms: FMoc-α-Me-Pro-OH;Fmoc-alpha-Me-L-Pro-OH;N-Fmoc-α-methyl-L-proline;1-Fmoc-2-methyl-L-proline;(S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)-2-methylpyrrolidine-2-carboxylic acid;Fmoc-a-Me-Pro-OH;(9H-Fluoren-9-yl)MethOxy]Carbonyl Alpha-Methyl-Pro-OH
• CAS NO: 167275-47-0
• Molecular Formula: C21H21NO4
• Molecular Weight: 351.39574
• EINECS: 200-582-5
• Product Categories: α-Methyl Amino Acids
• Mol File: 167275-47-0.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: FMoc-α-Me-Pro-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMoc-α-Me-Pro-OH(167275-47-0)
• EPA Substance Registry System: FMoc-α-Me-Pro-OH(167275-47-0)

Safety Data

• Hazard Codes: F,T
• Statements: 14/15-24/25-34
• Safety Statements: 26-36/37/39-43-45
• TSCA: No
• Hazardous Substances Data: 167275-47-0(Hazardous Substances Data)

Usage

General Description

FMoc-α-Me-Pro-OH is a chemical compound commonly used in peptide synthesis and solid-phase peptide synthesis. It is a derivative of α-Methyl-Proline and is often used as a protecting group for amino acids. FMoc-α-Me-Pro-OH is known for its stability and its ability to facilitate the purification and isolation of peptides. It can also be used as a reagent in the production of peptide and peptide-based drugs. The FMoc group is commonly used in peptide synthesis because of its ease of removal under mild conditions, making it a versatile tool for the creation of complex peptides. FMoc-α-Me-Pro-OH is an important compound for chemists and researchers working in the field of peptide chemistry and drug development.

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 109-70-6 1.3-chlorobromopropane 
• 42856-71-3 (S)-2-methylpyrrolidine-2-carboxylic acid 

Relevant articles and documents

A solid-phase synthetic route to unnatural amino acids with diverse side-chain substitutions

Reacting imine derivatives of resin-bound amino acids with α,ω-dihaloalkanes provides highly versatile intermediates to racemic α,α-disubstituted amino acids with a wide variety of side-chain functionality. Two strategies were developed to convert the int

Chemical scale studies of the Phe-Pro conserved motif in the cys loop of cys loop receptors

The functions of two conserved residues, Phe135 and Pro 136, located at the apex of the Cys loop of the nicotinic acetylcholine receptor are investigated. Both residues were substituted with natural and unnatural amino acids, focusing on the role of aromaticity at Phe135, backbone conformation at Pro136, side chain polarity and volume, and the specific interaction between the aromatic side chain and the proline. NMR spectroscopy studies of model peptides containing proline and unnatural proline analogues following a Phe show a consistent increase in the population of the cis conformer relative to peptides lacking the Phe. In the receptor, a strong interaction between the Phe and Pro residues is evident, as is a strong preference for aromaticity and hydrophobicity at the Phe site. A similar influence of hydrophobicity is observed at the proline site. In addition, across a simple homologous series of proline analogues, the results reveal a correlation between receptor function and cis bias at the proline backbone. This could suggest a significant role for the cis proline conformer at this site in receptor function.