144701-20-2

Usage

Uses

Used in Biochemistry Research:
FMOC-DL-NLE-OH is used as a protected amino acid for peptide synthesis, providing a stable and easily modifiable building block in the construction of complex peptide sequences.
Used in Peptide Synthesis:
FMOC-DL-NLE-OH is used as a key component in the synthesis of peptides, allowing for the controlled addition of amino acids to form specific peptide chains. The protective FMOC group ensures that the amino acid does not participate in unwanted side reactions during the synthesis process.
Used in Drug Development:
FMOC-DL-NLE-OH is used as a potential building block in the development of new pharmaceutical compounds, particularly in the creation of novel peptide-based drugs. Its unique structure and reactivity make it a valuable asset in the design and synthesis of therapeutic agents.
Used in Diagnostic Applications:
FMOC-DL-NLE-OH is used as a reagent in the development of diagnostic tools, such as immunoassays and biosensors, where its specific reactivity and stability can be exploited to detect or measure biological targets.

Upstream product

• 616-06-8 2-amino-hexanoic acid 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 327-56-0 D-norleucine 
• 327-57-1 L-Norleucine 
• 947154-63-4 2-N-fluorenylmethoxycarbonylaminohex-4-enoic acid 

Downstream Products

• 1062260-93-8 C₃₄H₄₂N₄O₆ 
• 1062260-89-2 C₃₃H₃₈N₄O₆ 
• 1062261-02-2 C₃₄H₄₂N₄O₆ 
• 1181341-93-4 H-Tyr-D-Ala-Gly-Phe-Nle-Pro-Leu-Ser(Glc)-Trp-NH-3,5-Bzl(CF₃)2 
• 1181341-91-2 H-Tyr-D-Ala-Gly-Phe-Nle-Ser(Glc)-Leu-Trp-NH-3,5-Bzl(CF₃)2 
• 1181341-92-3 H-Tyr-D-Ala-Gly-Phe-Nle-Pro-Ser(Glc)-Trp-NH-3,5-Bzl(CF₃)2 
• 244171-25-3 Ac-Nle-c[Asp-His-DPhe-Pro-Trp-Lys]-NH₂ 
• 1155867-00-7 Ac-Nle-c[Asp-trans-4-guanidinyl-Pro-DPhe-Arg-Trp-Lys]-NH₂ 
• 1155867-01-8 Ac-Nle-c[Asp-cis-4-guanidinyl-Pro-DPhe-Arg-Trp-Lys]-NH₂ 
• 1311485-32-1 [Nle₂₃]26RFa(20-26) 
• 1443329-22-3 H-Lys-c[Lys-Nle-Aib-Val-Glu]-Lys-Tyr-NH₂ 

Relevant academic research and scientific papers

Syntheses of Thailandepsin B Pseudo-Natural Products: Access to New Highly Potent HDAC Inhibitors via Late-Stage Modification

New Thailandepsin B pseudo-natural products have been prepared. Our synthetic strategy offers the possibility to introduce varying warheads via late stage modification. Additionally, it gives access to the asymmetric branched allylic ester moiety of the natural product in a highly diastereoselective manner applying rhodium-catalyzed hydrooxycarbonylation. The newly developed pseudo-natural products are extremely potent and selective HDAC inhibitors. The non-proteinogenic amino acid d-norleucine was obtained enantioselectively by a recently developed method of rhodium-catalyzed hydroamination.

Determination of Chemical and Enantiomeric Purity of α-Amino Acids and their Methyl Esters as N-Fluorenylmethoxycarbonyl Derivatives Using Amylose-derived Chiral Stationary Phases

Liquid chromatographic enantiomer separation and simultaneous determination of chemical and enantiomeric purity of α-amino acids and their methyl esters as N-fluorenylmethoxycarbonyl (FMOC) derivatives was performed on three covalently bonded type chiral stationary phases (CSPs) derived from amylose derivatives. The enantiomer separation of α-amino acid esters as N-FMOC derivatives was better than that of the corresponding acids, especially for CSP 1 and 2. Chemical impurities as the corresponding racemic acids present in several commercially available racemic amino acid methyl esters were observed to be 0.49–17.50%. Enantiomeric impurities of several commercially available L-amino acid methyl esters were found to be 0.03–0.58%, whereas chemical impurities as the corresponding racemic acids present in the same analytes were found to be 0.13–13.62%. This developed analytical method will be useful for the determination of chemical and enantiomeric purity of α-amino acids and/or esters as N-FMOC derivatives using amylose-derived CSPs.

AMINO ACID ANALOGUES AND METHODS FOR THEIR SYNTHESIS

A method for the synthesis of an amino acid analogue or a salt, solvate, derivative, isomer or tautomer thereof comprising the steps of: (i) subjecting an amino acid containing a metathesisable group to metathesis with a compound containing a complementary metathesisable group of formula (I) or (II): (Formulae (I), (II)) wherein R1 and R2 are independently selected from H and substituted or unsubstituted C1 to C4 alkyl; each R3 is either absent or independently selected from a heteroatom, a substituted or unsubstituted C1 to C20 alkyl, and a substituted or unsubstituted C1 to C20 alkyl group interrupted by one or more heteroatoms; and each X is independently selected from H and an effector molecule; in the presence of a reagent to catalyse the metathesis to form a dicarba bridge between the amino acid containing a metathesisable group and the compound containing a complementary metathesisable group; and (ii) reducing the dicarba bridge to form a saturated dicarba bridge, wherein the reagent used to catalyse step (i) also catalyses step (ii).

Tandem Ru-alkylidene-catalysed cross metathesis/hydrogenation: Synthesis of lipophilic amino acids

Highly efficient synthesis of lipidic amino acids can be achieved via Ru-alkylidene-catalysed cross metathesis of long chain alkenes with commercially available allylglycine. The resultant unsaturated analogues can be then optionally hydrogenated under mi

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

Novel peptides possessing a macrophage chemotactic activity

The present invention relates to physiologically active peptides and more particularly, to novel peptides having a specific amino acid sequence which possess a macrophage chemotactic activity.