202114-53-2

Basic information

• Product Name: FMOC-LEU-OH (C1-13C)
• Synonyms: L-LEUCINE-N-FMOC (1-13C);FMOC-LEU-OH (C1-13C);N-(9-FLUORENYLMETHOXYCARBONYL)-L-LEUCINE-1-13C;N-ALPHA-FMOC-L-LEUCINE (C1-13C);N-(9-FLUORENYLMETHOXYCARBONYL)-L-LEUCINE -1-13C, 99 ATOM % 13C;fmoc-leu-oh-1-13c;L-Leucine-1-13C, N-Fmoc, N-(9-Fluorenylmethoxycarbonyl)-L-leucine-1-13C;(2S)-2-{[(9H-fluoren-9-ylMethoxy)carbonyl]aMino}-4-Methylpentanoic acid
• CAS NO: 202114-53-2
• Molecular Formula: C21H23NO4
• Molecular Weight: 354.42
• Mol File: 202114-53-2.mol
• Article Data: 2

Chemical Properties

• Melting Point: 152-156 °C(lit.)
• Appearance: /
• CAS DataBase Reference: FMOC-LEU-OH (C1-13C)(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-LEU-OH (C1-13C)(202114-53-2)
• EPA Substance Registry System: FMOC-LEU-OH (C1-13C)(202114-53-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 202114-53-2(Hazardous Substances Data)

Usage

General Description

FMOC-LEU-OH (C1-13C) is a derivative of the amino acid leucine, in which the carbon at the first position is labeled with the 13C isotope. It is commonly used in solid-phase peptide synthesis as a building block for the construction of peptides and proteins. The FMOC group at the N-terminus of the molecule serves as a protecting group during synthesis, which can be easily removed under mild acidic conditions. The presence of the 13C label allows for the tracking of the labeled carbon atom in subsequent studies, making it useful for research in areas such as protein structure and dynamics, as well as metabolic studies. Overall, FMOC-LEU-OH (C1-13C) is a valuable tool for the study of peptides and proteins in biological and chemical research.

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 74292-94-7 (1-¹³C)-L-leucine 

Relevant articles and documents

Evaluation of dihedral angles of peptides using IR bands of two successive isotope labeled residues

The infrared (IR) absorption bands due to peptide bonds (amide bands) have long been used to determine the secondary structure of a peptide and to analyze intra- and intermolecular interactions between amides. In the present study, the dihedral angles of a residue in peptides have also been evaluated using the amide I IR band of two successive residues with isotope labeling. The two successive residues labeled with the13C and18O isotopes give the doublet amide I IR band and the intensity ratio (Rint) and the difference in peak position (|ν) of the doublet band were analyzed using GF matrix and ab initio molecular orbital calculations. We obtained the two-dimensional calculation maps of Rint and |ν against the two dihedral angles. The crossing point of the curves of Rint and |ν is the two dihedral angles of the measured residue. The evaluated dihedral angles of the simple peptides are compared with the reported values. We discuss the limitation and the application of the present method to biopolymers from the obtained results.