93372-25-9

Usage

Uses

Used in Chemical Synthesis:
FMOC-2,2,6,6-TETRAMETHYLPIPERIDINE-N-OXYL-4-AMINO-4-CARBOXYLIC ACID is used as a protected spin-labeled amino acid for chemical synthesis. Its enantiomerically pure state ensures the desired chirality in the final product, which is crucial for the biological activity and selectivity of the synthesized compounds.
Used in Biochemistry and Molecular Biology:
FMOC-2,2,6,6-TETRAMETHYLPIPERIDINE-N-OXYL-4-AMINO-4-CARBOXYLIC ACID is used as a stable free radical spin label in biochemistry and molecular biology. Its stable free radical allows for the investigation of molecular dynamics, protein structure, and protein-protein interactions through techniques such as electron paramagnetic resonance (EPR) spectroscopy.
Used in Pharmaceutical Industry:
FMOC-2,2,6,6-TETRAMETHYLPIPERIDINE-N-OXYL-4-AMINO-4-CARBOXYLIC ACID is used as a building block in the pharmaceutical industry for the development of novel drugs. Its unique structure and properties can be exploited to design and synthesize new drug candidates with improved pharmacological properties, such as enhanced potency, selectivity, and reduced side effects.
Used in Materials Science:
FMOC-2,2,6,6-TETRAMETHYLPIPERIDINE-N-OXYL-4-AMINO-4-CARBOXYLIC ACID is used as a component in the development of advanced materials in materials science. Its stable free radical nature can be utilized to create new materials with unique properties, such as enhanced stability, conductivity, or magnetic properties, for various applications, including sensors, catalysts, and energy storage devices.

Upstream product

• 15871-56-4 2',5'-Dioxo-2,2,6,6-tetramethyl-piperidin-(4-spiro-4')-imid-azolidin-oxyl-(1) 
• 45985-26-0 4-oxo-2,2,6,6-tetramethylpiperidin-oxyl 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 
• 15871-57-5 4-Amino-4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl radical 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 

Relevant academic research and scientific papers

Orientation of spin labels in de novo peptides

A series of de novo synthesised peptides including the artificial rigid paramagnetic amino acid TOAC at two positions with different distances from two to seven in the primary structure have been investigated by 9- and 94-GHz EPR spectroscopy under solid-state conditions. From simulations of the spectra of such two-spin systems, the distance and relative orientation of the paramagnetic centres can be deduced. This yields structural information on the peptides. A quantitative analysis of the spectra of individual peptides in different solvents as well as a qualitative analysis of the spectra of the peptide series shows that the peptides do not assume conformations corresponding to any of the common helical structures in proteins. Copyright

α-helical versus 310-helical conformation of alanine-based peptides in aqueous solution: An electron spin resonance investigation

Due to the difficulties in experimentally differentiating between the α- and 310-helical conformations in solution, isolated helical peptides have been assumed to be in the α-helical conformation. However, recent electron spin resonance (ESR) studies have suggested that such peptides, in particular short alanine-based peptides, are 310-helical (Miick, S. M.; et al. Nature 1992, 359, 653-5). This result prompted us to further investigate the helical conformations of alanine-based peptides in solution using electron spin resonance spectroscopy. Unlike previous investigations with a flexible link connecting the spin-label to the peptide backbone, we used a conformationally constrained spin-label (4-amino-4-carboxy-2,2,6,6-tetramethylpiperidine-1-oxyl, Toac) that is rigidly attached to the peptide backbone. From a combination of molecular modeling and ESR spectroscopy investigations, it was concluded that these alanine-based peptides exist primarily in the α-helical conformation, and not the 310-form as previously suggested for an analogous set of peptides in aqueous environments. This discrepancy is thought to be due to the differences in flexibility of the spin-labels employed. The conformationally constrained spin-label Toac used in this study should accurately reflect the backbone conformation. Free energy surfaces, or potentials of mean force, for the conformational transition of the spin-label used in previous studies (Miick S. M.; et al. Nature 1992, 359, 653-5) suggest that this spin-label is too flexible to accurately distinguish between the α- and 310-helical conformations.