198560-44-0

Basic information

• Product Name: Fmoc-3-chloro-L-phenylalanine
• Synonyms: (L)-3-CHLOROPHENYL-N-FMOC-ALANINE;FMOC-3-CHLORO-L-PHENYLALANINE;FMOC-L-3-CHLOROPHE;FMOC-L-3-CHLOROPHENYLALANINE;FMOC-PHE(3-CL)-OH;FMOC-PHE(M-CL)-OH;FMOC-L-PHE(3-CL)-OH;FMOC-M-CHLORO-L-PHE-OH
• CAS NO: 198560-44-0
• Molecular Formula: C24H20ClNO4
• Molecular Weight: 421.87
• Product Categories: Amino Acids;Phenylalanine analogs and other aromatic alpha amino acids;Peptide;a-amino
• Mol File: 198560-44-0.mol

Chemical Properties

• Boiling Point: 640.9 °C at 760 mmHg
• Flash Point: 341.4 °C
• Appearance: /Solid
• Density: 1.337 g/cm³
• Vapor Pressure: 2.64E-17mmHg at 25°C
• Refractive Index: 1.637
• Storage Temp.: Store at 0°C
• PKA: 3.70±0.10(Predicted)
• CAS DataBase Reference: Fmoc-3-chloro-L-phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-3-chloro-L-phenylalanine(198560-44-0)
• EPA Substance Registry System: Fmoc-3-chloro-L-phenylalanine(198560-44-0)

Safety Data

• Hazard Codes: Xi
• HazardClass: IRRITANT
• Hazardous Substances Data: 198560-44-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Fmoc-3-chloro-L-phenylalanine is used as a building block for the synthesis of peptides and proteins, facilitating the development of new drug molecules. Its incorporation into peptide structures allows for the exploration of peptide-ligand interactions, which is vital for understanding and enhancing drug efficacy and specificity.
Used in Biochemical Research:
In biochemical research, Fmoc-3-chloro-L-phenylalanine is utilized as a component in solid-phase peptide synthesis. This method is essential for studying the interactions between peptides and their target molecules, contributing to a deeper understanding of biological processes and the discovery of novel therapeutic agents.
Used in Peptide Synthesis:
Fmoc-3-chloro-L-phenylalanine is used as a key component in the synthesis of specific peptides, particularly those requiring the unique properties conferred by the 3-chloro substituent. This allows for the creation of peptides with tailored characteristics, useful in various applications such as diagnostics, therapeutics, and research tools.

InChI:InChI=1/C24H20ClNO4/c25-16-7-5-6-15(12-16)13-22(23(27)28)26-24(29)30-14-21-19-10-3-1-8-17(19)18-9-2-4-11-20(18)21/h1-12,21-22H,13-14H2,(H,26,29)(H,27,28)/t22-/m0/s1

Upstream product

• 1956-15-6 3-chlorophenylalanine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 123053-22-5 (S)-3-chlorophenylalanine hydrochloride 

Downstream Products

• 1610618-51-3 C₃₉H₄₅ClN₆O₄ 

Relevant articles and documents

METHOD FOR PREPARING AROMATIC AMINO ACID DERIVATIVE

The present invention provides methods of efficiently producing various optically active aromatic amino acid derivatives by reacting, using an additive, a specific ester compound with an aromatic halide and zinc in the presence of a catalyst. The present invention also provides amino acid derivatives that can be produced by the methods.

synthesis of both enantiomers of chiral phenylalanine derivatives catalyzed by cinchona alkaloid quaternary ammonium salts as asymmetric phase transfer catalysts

A practical synthesis of both enantiomers of unnatural phenylalanine derivatives by using two pseudoenantiomeric phase transfer catalysts is described. Through asymmetric α-alkylation of glycine Schiff base with substituted benzyl bromides and 1-(bromomet

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