1219145-37-5

Basic information

• Product Name: FMOC-2-AMINO-4,4,4-TRIFLUOROBUTYRIC ACID
• Synonyms: FMOC-2-AMINO-4,4,4-TRIFLUOROBUTYRIC ACID;2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-4,4,4-trifluorobutanoic acid
• CAS NO: 1219145-37-5
• Molecular Formula: C19H16F3NO4
• Molecular Weight: 379.33
• Mol File: 1219145-37-5.mol
• Article Data: 5

Chemical Properties

• Appearance: /
• CAS DataBase Reference: FMOC-2-AMINO-4,4,4-TRIFLUOROBUTYRIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-2-AMINO-4,4,4-TRIFLUOROBUTYRIC ACID(1219145-37-5)
• EPA Substance Registry System: FMOC-2-AMINO-4,4,4-TRIFLUOROBUTYRIC ACID(1219145-37-5)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 1219145-37-5(Hazardous Substances Data)

Usage

Uses

2-[[(9H-Fluoren-9-ylmethoxy)carbonyl]amino]-4,4,4-trifluorobutanoic acid is used in the synthesis of heterocyclic and aromatic ureas and amides as CEPT inhibitors.

Upstream product

• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 262296-39-9 C₄H₆F₃NO₂*ClH 
• 15960-05-1 α-amino-γ,γ,γ-trifluorobutyrate 

Relevant articles and documents

Preparative Method for Asymmetric Synthesis of (S)-2-Amino-4,4,4-trifluorobutanoic Acid

Enantiomerically pure derivatives of 2-amino-4,4,4-trifluorobutanoic acid are in great demand as bioisostere of leucine moiety in the drug design. Here, we disclose a method specifically developedforlarge-scale(>150g)preparationofthetarget(S)-N-Fmoc-2-ami

TUBULYSIN ANALOGUES AS ANTICANCER AGENTS AND PAYLOADS FOR ANTIBODY-DRUG CONJUGATES AND METHODS OF TREATMENT THEREWITH

In one aspect, the present disclosure provides tubulysin analogs of the formula (I) wherein the variables are as defined herein. In another aspect, the present disclosure also provides methods of preparing the compounds disclosed herein. In another aspect

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