198560-43-9

Basic information

• Product Name: FMOC-L-3,4-Difluorophe
• Synonyms: FMOC-PHE(3,4-F2)-OH;FMOC-PHE(3,4-DIF)-OH;FMOC-PHE(M,P-F2)-OH;Fluorenylmethoxycarbonyl-L-3,4-difluorophenylalanine;FMOC-3,4-DIFLUORO-L-PHENYLALANINE;FMOC-3,4-DIFLUORO-L-PHE-OH;FMOC-L-PHE(3,4-F2)-OH;FMOC-L-3,4-DIFLUOROPHE
• CAS NO: 198560-43-9
• Molecular Formula: C24H19F2NO4
• Molecular Weight: 423.41
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Amino Acid Derivatives;Peptide
• Mol File: 198560-43-9.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 622.7 °C at 760 mmHg
• Flash Point: 330.4 °C
• Appearance: /
• Density: 1.357 g/cm³
• Storage Temp.: 2-8°C
• PKA: 3.68±0.10(Predicted)
• BRN: 8947230
• CAS DataBase Reference: FMOC-L-3,4-Difluorophe(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-L-3,4-Difluorophe(198560-43-9)
• EPA Substance Registry System: FMOC-L-3,4-Difluorophe(198560-43-9)

Safety Data

• Hazard Codes: Xi
• WGK Germany: 3
• Hazardous Substances Data: 198560-43-9(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Upstream product

• 32133-36-1 2-amino-3-(3,4-difluorophenyl)propanoic acid 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 

Relevant articles and documents

Novel selective inhibitors of the interaction of individual nuclear hormone receptors with a mutually shared steroid receptor coactivator 2

Nuclear hormone receptor (NR) signaling, currently a therapeutic target in multiple diseases, involves an ordered series of protein interactions to regulate transcription in response to changing hormone levels. Later steps in the process of ligand-dependent signaling are driven by a highly conserved interaction between the NRs and the steroid receptor coactivators (SRCs) that is effected by a conserved interaction motif (L1XXL2L3), known as an NR box. Using computational design and combinatorial chemistry, we have produced novel ∞-helical proteomimetics of the second NR box of SRC2 that exploit structural differences between human estrogen receptor ∞ (hER∞), human estrogen receptor β (hERβ), and human thyroid hormone receptor β (hTRβ). The resulting library sequentially replaced each leucine with non-natural side chains. Screening this library using a quantitative competition assay revealed compounds that selectively inhibit the interaction of SRC2-2 with each individual NR in preference to its interaction with the other NR. This approach generated highly selective compounds from one that had no specificity for a particular family member. These compounds represent the first family-member-selective competitive inhibitors of the protein interactions of transcription factors. Copyright