181128-48-3

Usage

Uses

Used in Medicinal Chemistry:
(S)-Fmoc-2-amino-4,4,4-trifluoro-butyric acid is used as a building block for the synthesis of complex peptides and other biomolecules in the field of medicinal chemistry. Its Fmoc protective group ensures that the molecule remains stable during the synthesis process, while the trifluoro-butyric acid chain provides a unique structural feature that can be exploited for the development of novel therapeutic agents.
Used in Peptide Synthesis:
In the field of peptide synthesis, (S)-Fmoc-2-amino-4,4,4-trifluoro-butyric acid is used as a key component in the construction of peptide sequences. The Fmoc group serves as a temporary protective layer that shields the molecule from unwanted reactions, allowing for precise and controlled synthesis of peptides with specific properties and functions.
Used in Drug Development:
(S)-Fmoc-2-amino-4,4,4-trifluoro-butyric acid is employed as a versatile chemical intermediate in the development of new drugs. Its unique structure and the presence of the Fmoc protective group make it a valuable asset in the design and synthesis of potential therapeutic agents, particularly in the realm of peptide-based drugs.
Used in Scientific Research:
In the broader context of scientific research, (S)-Fmoc-2-amino-4,4,4-trifluoro-butyric acid is used as a reagent and a tool for studying various biological processes and interactions. Its chiral nature and the presence of the trifluoro-butyric acid chain make it an interesting subject for research in areas such as biochemistry, molecular biology, and structural biology.

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 academic research and scientific papers

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

Expedient Asymmetric Synthesis of (S)-2-Amino-4,4,4-trifluorobutanoic Acid via Alkylation of Chiral Nucleophilic Glycine Equivalent

Here we disclose a practical asymmetric synthesis of an enantiomerically 97.8% ee pure N-Fmoc derivative of (S)-2-amino-4,4,4-trifluorobutanoic acid performed on >10 g scale of the target product. The method is based on alkylation (CF3-CH2-I) of a new generation of a chiral nucleophilic equivalent conducted at ambient temperature with an excellent stereochemical outcome. The developed protocol does not require any chromatographic separations and includes only one purification step via recrystallization of the final product.

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

Improved Total Synthesis of Tubulysins and Design, Synthesis, and Biological Evaluation of New Tubulysins with Highly Potent Cytotoxicities against Cancer Cells as Potential Payloads for Antibody-Drug Conjugates

Improved, streamlined total syntheses of natural tubulysins such as V (Tb45) and U (Tb46) and pretubulysin D (PTb-D43), and their application to the synthesis of designed tubulysin analogues (Tb44, PTb-D42, PTb-D47-PTb-D49, and Tb50-Tb120), are described.

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