188632-07-7

Basic information

• Product Name: FMOC-DL-CHA-OH
• Synonyms: FMoc-3-Cyclohexylalanine;3-Cyclohexyl-N-[(9H-fluoren-9-ylmethoxy)carbonyl]alanine
• CAS NO: 188632-07-7
• Molecular Formula: C₂₄H₂₇NO₄
• Molecular Weight: 393.48
• Mol File: 188632-07-7.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: FMOC-DL-CHA-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-DL-CHA-OH(188632-07-7)
• EPA Substance Registry System: FMOC-DL-CHA-OH(188632-07-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 188632-07-7(Hazardous Substances Data)

Usage

General Description

FMOC-DL-CHA-OH is a chemical compound consisting of an FMOC (9-fluorenylmethoxycarbonyl) protecting group attached to a DL-CHA (DL-cyclohexylalanine) amino acid. The FMOC group is commonly used in peptide synthesis to protect the amine group of amino acids and facilitate peptide purification. DL-CHA is a chiral amino acid with a cyclohexane ring in its side chain, and it has been used in the synthesis of peptidomimetics and pharmaceutical compounds. FMOC-DL-CHA-OH is often utilized in solid-phase peptide synthesis and has potential applications in drug development and medical research as a building block for the synthesis of bioactive peptides. Additionally, the compound may also be used in the study of structure-activity relationships in peptide-based compounds.

Upstream product

• 4441-50-3 β-cyclohexylalanine 
• 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