409333-67-1

Usage

Uses

Used in Peptide Synthesis:
BOC-D,L-5,5,5-TRIFLUOROLEUCINE is used as a building block for peptide synthesis, where the BOC-protecting group can be removed under mild acid conditions to expose the amino group for subsequent peptide coupling reactions. This feature is crucial for the stepwise assembly of complex peptide structures.
Used in Bioactive Peptide Design:
In the pharmaceutical and biotechnology industries, BOC-D,L-5,5,5-TRIFLUOROLEUCINE is used as a key component in the design of bioactive peptides. The trifluoroleucine moiety contributes to the hydrophobicity and stereochemistry of the peptides, which can influence their biological activity and selectivity.
Used in Research and Development:
BOC-D,L-5,5,5-TRIFLUOROLEUCINE is utilized in research settings for the exploration of novel peptide-based therapeutics and the study of peptide structure-function relationships. Its unique properties allow scientists to investigate the effects of specific amino acid modifications on peptide behavior and activity.
Overall, BOC-D,L-5,5,5-TRIFLUOROLEUCINE is a versatile chemical compound with significant applications in the synthesis and design of peptides, contributing to advancements in medicine, biotechnology, and chemical research.

InChI:InChI=1/C11H18F3NO4/c1-6(11(12,13)14)5-7(8(16)17)15-9(18)19-10(2,3)4/h6-7H,5H2,1-4H3,(H,15,18)(H,16,17)

Upstream product

• 93267-04-0 N-(tert-butoxycarbonyl)-L-3-iodoalanine methyl ester 
• 24424-99-5 di-tert-butyl dicarbonate 
• 2792-72-5 2-amino-4-methyl-5,5,5-trifluoropentanoic acid 
• 120097-69-0 (DL)-2-(N-acetylamino)-4-methyl-5,5,5-trifluoropentanoic acid 

Downstream Products

• 1443124-52-4 C₁₈H₂₄F₃NO₄ 
• 1443124-51-3 (2S)-N-Boc-5,5,5-trifluoroleucine benzyl ester 

Relevant academic research and scientific papers

Palladium-catalyzed cross-coupling of unactivated alkylzinc reagents with 2-bromo-3,3,3-trifluoropropene and its application in the synthesis of fluorinated amino acids

A palladium-catalyzed cross-coupling of unactivated alkylzinc reagents with 2-bromo-3,3,3-trifluoropropene (BTP) has been developed, which was used as a key step to prepare a series of trifluoromethylated and difluoromethylated amino acids that are of great interest in peptide/protein based chemical biology. The advantages of the synthesis of these fluorinated amino acids are synthetic simplicity and diversity from a simple and readily available key intermediate α-trifluoromethylalkene-containing amino acid, providing a facile route for applications in medicinal chemistry and life science.

MODULATORS OF SESTRIN-GATOR2 INTERACTION AND USES THEREOF

The present invention provides compounds, compositions thereof, and methods of using the same.

MODULATORS OF SESTRIN-GATOR2 INTERACTION AND USES THEREOF

The present invention provides compounds, compositions thereof, and methods of using the same.

Non-racemic hexafluoreleucine, and methods of making and using it

One aspect of the invention relates to hexafluoroleucine and congeners thereof, and methods of making the compounds. Another aspect of the nvention relates to the synthesis of protein cores comprising hexafluoroleucine and congeners thereof. Certain peptides comprising hexafluorleucine and congeners thereof have been characterized using comparative biophysical studies. In general, the fluorinated peptides show higher thermal stability and enhanced resistance to chemical denaturation. Further, mixed hydrocarbonfluorocarbon cores self-sort into homogeneous bundles, suggesting new avenues for the design and manipulation of protein-protein interfaces.

A coiled coil with a fluorous core

The design, synthesis, and structural characterization of a highly fluorinated peptide system based on the coiled coil region of the yeast transcription factor GCN4 is described. All four leucine residues (a position) and three valine residues (d position) were replaced by the unnatural amino acids 5,5,5-trifluoroleucine and 4,4,4-trifluorovaline, respectively. The peptide is highly α-helical at low micromolar concentrations as judged by circular dichroism spectra, sediments as a dimeric species in the 5-30 μM concentration range, and exhibits a dimer melting temperature that is 15 °C higher than a control peptide with a hydrocarbon core. Furthermore, the apparent free energy of unfolding as calculated from guanidinium hydrochloride denaturation experiments is larger by ～1.0 kcal/mol for the fluorinated peptide than its hydrocarbon counterpart. We conclude that additional stability is derived from sequestering the more hydrophobic trifluoromethyl groups from aqueous solvent. These studies introduce a new paradigm in the design of molecular self-assembling systems, one based on orthogonal solubility properties of liquid phases.