84000-07-7

Basic information

• Product Name: FMOC-N-Methyl-L-alanine
• Synonyms: FMOC-L-MEALA-OH;FMOC-N-ALPHA-METHYL-L-ALANINE;FMOC-MEALA-OH;FMOC-N-METHYL-L-ALANINE;FMOC-N-ME-ALA-OH;FMOC-N-ME-L-ALA-OH;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-N-ALPHA-METHYL-L-ALANINE;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-N-ALPHA-METHYL-L-ALANINE
• CAS NO: 84000-07-7
• Molecular Formula: C₁₉H₁₉NO₄
• Molecular Weight: 325.36
• EINECS: 1533716-785-6
• Product Categories: Amino Acids;Alanine [Ala, A];N-Methyl Amino Acids;Fmoc-Amino acid series
• Mol File: 84000-07-7.mol

Chemical Properties

• Melting Point: ~150 °C
• Boiling Point: 514.9 °C at 760 mmHg
• Flash Point: 265.2 °C
• Appearance: /Solid
• Density: 1.262 g/cm³
• Vapor Pressure: 1.99E-11mmHg at 25°C
• Refractive Index: 1.604
• Storage Temp.: 2-8°C
• PKA: 3.92±0.10(Predicted)
• Water Solubility: Slightly soluble in water.
• BRN: 4329998
• CAS DataBase Reference: FMOC-N-Methyl-L-alanine(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-N-Methyl-L-alanine(84000-07-7)
• EPA Substance Registry System: FMOC-N-Methyl-L-alanine(84000-07-7)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• HazardClass: IRRITANT
• Hazardous Substances Data: 84000-07-7(Hazardous Substances Data)

Usage

Uses

Used in Peptide Synthesis:
FMOC-N-Methyl-L-alanine is used as a building block in peptide synthesis for the incorporation of N-methyl amino acids into peptide sequences. The presence of the Fmoc group allows for the selective deprotection and coupling of the amino acid during the synthesis process, facilitating the assembly of complex peptide structures.
Used in Pharmaceutical Industry:
FMOC-N-Methyl-L-alanine is used as an intermediate in the synthesis of various pharmaceutical compounds. The N-methylation of amino acids can lead to changes in the pharmacological properties of the resulting compounds, such as increased lipophilicity, enhanced membrane permeability, and altered binding affinity to target proteins. This makes FMOC-N-Methyl-L-alanine a valuable component in the development of new drugs with improved efficacy and selectivity.
Used in Agrochemical Industry:
FMOC-N-Methyl-L-alanine is utilized as a key intermediate in the synthesis of agrochemicals, such as pesticides and herbicides. The introduction of the N-methyl group can enhance the biological activity and selectivity of these compounds, leading to more effective and environmentally friendly agricultural products.
Used in Dye Industry:
FMOC-N-Methyl-L-alanine is employed as a starting material or intermediate in the production of various dyes and pigments. The unique chemical properties of this amino acid derivative can contribute to the development of novel dyes with improved colorfastness, stability, and application properties.

InChI:InChI=1/C19H19NO4/c1-12(18(21)22)20(2)19(23)24-11-17-15-9-5-3-7-13(15)14-8-4-6-10-16(14)17/h3-10,12,17H,11H2,1-2H3,(H,21,22)/t12-/m0/s1

Upstream product

• 83999-95-5 9H-fluoren-9-ylmethyl (S)-4-methyl-5-oxo-1,3-oxazolidine-3-carboxylate 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 65672-32-4 N-methyl-L-alanine hydrochloride 
• 3913-67-5 N-methylalanine 
• 50-00-0 formaldehyd 
• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 693-13-0 diisopropyl-carbodiimide 
• 1220527-64-9 N-Fmoc-N-methyl-L-alanine benzhydyl ester 
• 1208119-53-2 N-methyl-N-nosyl-L-alanine phenacyl ester 
• 186581-53-3 diazomethane 
• 59724-75-3 N-(p-nitrophenylsulfonyl)-(S)-alanine 
• 67-56-1 methanol 
• 56-41-7 L-alanin 

Downstream Products

• 1195983-88-0 H-MeAla-Phe-Leu-NH₂ 
• 1195983-94-8 C₂₃H₃₇N₅O₄ 
• 1195983-93-7 C₂₈H₃₉N₅O₅ 
• 1195983-92-6 H-Tyr-MeAla-MeAla-Phe-Leu-NH₂ 

Relevant articles and documents

Total synthesis of hytramycin V, an antibiotic cyclopeptide

The total synthesis of the piperazic acid-containing antibiotic cyclic peptide, hytramycin V, has been achieved. Unexpected cleavage of the peptide bond was observed during the synthesis of a pentapeptide, we then successfully found that the addition of 2,6-di-tert-butylpyridine (2,6-DTBP) was effective to prevent the cleavage upon acylation with AgCN, leading to a pentapeptide in excellent yield. The synthesis of a hexapeptide, followed by global deprotection of the protecting groups provided a cyclization precursor. Finally, macrolactamization of the precursor using T3Pμ under high-dilution conditions furnished the desired natural product, hytramycin V. The synthesis of the enantiomer of hytramycin V was also achieved, and no difference between the enantiomers was observed in the evaluation of their antibacterial activity against Mycobacterium strains, revealing the fact that the potency of the activity was not dependent on the chirality of the cyclopeptide backbone.

INHIBITORS OF ENCEPHALITIC ALPHAVIRUSES

Compounds of Formula I and Formula II: pharmaceutical compositions containing them, and use of the compounds as active ingredients to treat infection with alphavirus.

Investigation for the cyclization efficiency of linear tetrapeptides: Synthesis of tentoxin B and dihydrotentoxin

Investigation of the cyclization efficiency of N-methyl linear tetrapeptides using a molecular modeling study and chemical synthesis is described. The linear peptide with two N-methyl groups, MeAla-Leu-MePhe-Gly, forms γ-turn like conformation with the am

CycLS: Accurate, whole-library sequencing of cyclic peptides using tandem mass spectrometry

Cyclic peptides are of great interest as therapeutic compounds due to their potential for specificity and intracellular activity, but specific compounds can be difficult to identify from large libraries without resorting to molecular encoding techniques. Large libraries of cyclic peptides are often DNA-encoded or linearized before sequencing, but both of those deconvolution strategies constrain the chemistry, assays, and quantification methods which can be used. We developed an automated sequencing program, CycLS, to identify cyclic peptides contained within large synthetic libraries. CycLS facilitates quick and easy identification of all library-members via tandem mass spectrometry data without requiring any specific chemical moieties or modifications within the library. Validation of CycLS against a library of 400 cyclic hexapeptide peptoid hybrids (peptomers) of unique mass yielded a result of 95% accuracy when compared against a simulated library size of 234,256 compounds. CycLS was also evaluated by resynthesizing pure compounds from a separate 1800-member library of cyclic hexapeptides and hexapeptomers with high mass redundancy. Of 22 peptides resynthesized, 17 recapitulated the retention times and fragmentation patterns assigned to them from the whole-library bulk assay results. Implementing a database-matching approach, CycLS is fast and provides a robust method for sequencing cyclic peptides that is particularly applicable to the deconvolution of synthetic libraries.

A new GLP-1 analogue with prolonged glucose-lowering activity in vivo via backbone-based modification at the N-terminus

Glucagon-like peptide-1 (GLP-1) is an endogenous insulinotropic hormone with wonderful glucose-lowering activity. However, its clinical use in type II diabetes is limited due to its rapid degradation at the N-terminus by dipeptidyl peptidase IV (DPP-IV). Among the N-terminal modifications of GLP-1, backbone-based modification was rarely reported. Herein, we employed two backbone-based strategies to modify the N-terminus of tGLP-1. Firstly, the amide N-methylated analogues 2-6 were designed and synthesized to make a full screening of the N-terminal amide bonds, and the loss of GLP-1 receptor (GLP-1R) activation indicated the importance of amide H-bonds. Secondly, with retaining the N-terminal amide H-bonds, the β-peptide replacement strategy was used and analogues 7-13 were synthesized. By two rounds of screening, analogue 10 was identified. Analogue 10 greatly improved the DPP-IV resistance with maintaining good GLP-1R activation in vitro, and showed approximately a 4-fold prolonged blood glucose-lowering activity in vivo in comparison with tGLP-1. This modification strategy will benefit the development of GLP-1-based anti-diabetic drugs.

GLP-1 PRODRUGS

The invention relates to a GLP-1 prodrug of the general formula I: R1-(NHXaa1)-Xaa2-(OHis)-(GLP-1 peptide) (Formula I), wherein GLP-1 peptide is GLP-1(8-37) (SEQ ID NO: 1) or an analogue thereof having a maximum of nine amino acid changes as compared to GLP-1(8-37), R1 is lower alkyl, (NHXaa1) is an amino acid, Xaa2 is an amino acid, and (OHis) is a radical of imidazole-lactic acid; or a pharmaceutically acceptable salt, amide, or ester of the prodrug. The invention also relates to specific GLP-1 parent drugs of the general formula II: (HOHis)-(GLP-1 peptide) (Formula II), as well as specific intermediate products. The invention furthermore relates to a method of achieving release in vivo of an active and stabilised GLP-1 parent drug of the general formula II: (HOHis)-(GLP-1 peptide), by administering a GLP-1 prodrug; as well as to such GLP-1 prodrug, and such GLP-1 parent drug, respectively, for use as a medicament, in particular for use in the treatment and/or prevention of all forms of diabetes and related diseases. The prodrug may be used to alter the PK and/or absorption profile of the drug, for example to a desirable bell-shaped curve. The parent drug has a good biological activity, and is stabilised against degradation by DPP-IV.

Total synthesis of proposed structure of coibamide A, a highly N- and O-methylated cytotoxic marine cyclodepsipeptide

Total synthesis of the originally proposed structure of coibamide A, a highly N- and O-methylated cytotoxic marine cyclodepsipeptide, has been accomplished by using a [(4+1)+3+3]-peptide fragment-coupling strategy and careful examination and optimization

MAYTANSINOID DERIVATIVES

Disclosed herein are maytansinoid drug linker derivatives which can be linked to a antigen binding unit (Abu), and maytansinoid drugs linked with an antigen binding unit (Drug-Linker-Antigen binding Unit: D-L-Abu), for targeted delivery to disease tissues. D-L-Abu, D-L-Abu derivatives, and methods relating to the use of such drug conjugates to treat antigen positive cells in cancers and immunological disorders are provided.

Fluorenylmethoxycarbonyl-N-methylamino acids synthesized in a flow tube-in-tube reactor with a liquid-liquid semipermeable membrane

Both steps of the N-methylation of 9-fluorenylmethoxycarbonyl (Fmoc) amino acids were carried out in a microstructured tube-in-tube reactor equipped with a semipermeable Teflon AF 2400 membrane as the inner tubing. In the first step, gaseous formaldehyde

Solid phase total synthesis of callipeltin e isolated from marine sponge Latrunculia sp.

Solid phase total synthesis of callipeltin E (1), truncated linear peptide isolated from marine sponge, Latrunculia sp. was achieved. Our strategy based on traditional Fmoc-SPPS was in common use TFA-treatment final deprotection to reach callipeltin E (1) contained acid-sensitive βMeOTyr.