16198-60-0

Basic information

• Product Name: HEXAFLUOROLEUCINE
• Synonyms: HEXAFLUOROLEUCINE;2-AMINO-5,5,5-TRIFLUORO-4-TRIFLUOROMETHYL-PENTANOIC ACID;Hexafluoroleucine 97%;Hexafluoroleucine97%;2-Amino-5,5,5-trifluoro-4-trifluoromethyl-pentanoic acid HCl;Hexafluoro-DL-leucine;2-Amino-5,5,5-trifluoro-4-trifluoromethyl pentanoic acid hydrochloride
• CAS NO: 16198-60-0
• Molecular Formula: C6H7F6NO2
• Molecular Weight: 239.12
• Product Categories: pharmacetical
• Mol File: 16198-60-0.mol

Chemical Properties

• Melting Point: >220°C
• Boiling Point: 224.672°C at 760 mmHg
• Flash Point: 89.679°C
• Appearance: /
• Density: 1.473g/cm³
• Vapor Pressure: 0.033mmHg at 25°C
• Refractive Index: 1.362
• CAS DataBase Reference: HEXAFLUOROLEUCINE(CAS DataBase Reference)
• NIST Chemistry Reference: HEXAFLUOROLEUCINE(16198-60-0)
• EPA Substance Registry System: HEXAFLUOROLEUCINE(16198-60-0)

Safety Data

• Hazard Codes: Xi
• HazardClass: IRRITANT
• Hazardous Substances Data: 16198-60-0(Hazardous Substances Data)

Usage

Uses

Used in Biochemical Research:
Hexafluoroleucine is used as a research tool for investigating the effects of fluorination on protein structure and function. Its incorporation into proteins can lead to more precise structural determination or induce conformational changes, offering insights into protein folding, dynamics, and stability.
Used in Structural Studies of Proteins:
In the field of structural biology, hexafluoroleucine is used as a substitute for leucine to probe the influence of fluorination on the three-dimensional structure of proteins. This can aid in understanding how protein conformation is affected by the presence of fluorine atoms, which is crucial for deciphering the mechanisms of protein function and interactions.
Used in Laboratory Settings:
Due to its synthetic nature and potential toxicity, hexafluoroleucine is used as a specialized reagent in controlled laboratory environments. Its application is limited to scientific research where its unique properties can be harnessed to advance our understanding of protein structure and function.

InChI:InChI=1/C6H7F6NO2/c1-4(2,7)6(9,10)5(8,3(14)15)13(11)12/h1-2H3,(H,14,15)

Upstream product

• 16063-98-2 2-amino-5,5,5-trifluoro-4-(trifluoromethyl)pentanoic acid 
• 478548-21-9 tert-butyl (2S)-2-[[(benzyloxy)carbonyl]amino]-5,5,5-trifluoro-4-(trifluoromethyl)pentanoate 
• 1053719-24-6 oxalic acid 3-benzyloxycarbonylamino-3-tert-butoxycarbonyl-1,1-bis-trifluoromethyl-propyl ester phenyl ester 
• 478548-20-8 tert-butyl (2S)-2-[[(benzyloxy)carbonyl]amino]-5,5,5-trifluoro-4-hydroxy-4-(trifluoromethyl)pentanoate 
• 201930-83-8 5,5,5-trifluoro-2-oxo-4-trifluoromethyl-pentanoic acid ethyl ester 

Downstream Products

• 149560-64-5 (S)-5,5,5,5',5',5'-hexafluoroleucine 
• 918667-71-7 (S)-2-{[((9H-fluoren-9-yl)methoxy)carbonyl]amino}-5,5,5-trifluoro-4-(trifluoromethyl)-pentanoic acid 

Relevant articles and documents

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.

Chemoenzymatic synthesis of (S)-hexafluoroleucine and (S)- tetrafluoroleucine

We have developed a short chemoenzymatic synthesis for both (S)-5,5,5,5′,5′,5′-hexafluoroleucine (Hfl) and (S)-5,5,5′,5′-tetrafluoroleucine (Qfl) on gram scale. Qfl was incorporated into a peptide using standard solid-phase peptide synthesis protocols to measure its helix propensity. The helix propensity for Qfl is 0.68 kcal·mol-1 more favorable compared to Hfl.

Helix propensity of highly fluorinated amino acids

Highly fluorinated amino acids have been used to stabilize helical proteins for potential application in various protein-based biotechnologies. To gain further insight into the effect of these highly fluorinated amino acids on helix formation exclusively, we measured the helix propensity of three highly fluorinated amino acids: (S)-5,5,5,5′,5′,5′-hexafluoroleucine (Hfl), (S)-2-amino-4,4,4-trifluorobutyric acid (Atb), and (S)-pentafluorophenylalanine (Pff). We have developed a short chemoenzymatic synthesis of Hfl with extremely high enantioselectivity (>99%). To measure the helix propensity (w) of the amino acids, alanine-based peptides were synthesized, purified, and investigated by circular dichroism spectroscopy (CD). On the basis of the CD data, the helix propensity of hydrocarbon amino acids can decrease up to 24-fold (1.72 kcal·mol-1·residue-1) upon fluorination. This difference in helix propensity has previously been overlooked in estimating the magnitude of the fluoro-stabilization effect (which has been estimated to be 0.32-0.83 kcal·mol-1·residue-1 for Hfl), resulting in a gross underestimation. Therefore, the full potential of the fluoro-stabilization effect should provide even more stable proteins than the fluoro-stabilized proteins to date. Copyright

Process for preparing single enantiomers of 5,5,5,5',5',5'-hexafluoroleucine and protected analogs

A process for synthesizing L and D-5,5,5,5′,5′,5′-hexafluoroleucine and protected analogs is disclosed. These compounds have utility in the preparation of fluorous peptides and proteins, which display interesting and unusual properties including strong self-association and an affinity for lipid bilayers.

A short and efficient synthesis of L-5,5,5,5',5',5'-hexafluoroleucine from N-Cbz-L-serine.

[reaction: see text] 5,5,5,5',5',5'-Hexafluoroleucine (6), a fluorous analogue of leucine, is of considerable interest as a building block in the design of fluorous proteins and peptides. We report a short and efficient synthesis of 6, which is obtained f