66866-67-9

Basic information

• Product Name: N-METHYL-L-PHENYLALANINE HYDROCHLORIDE
• Synonyms: N-a-methyl-L-Phenylalaninehydrochloride;-α-methyl-L-Phenylalanine hydrochloride;(S)-2-(methylamino)-3-phenylpropanoic acid hydrochloride;L-Phenylalanine, N-Methyl-, hydrochloride;H-MePhe-OH·HCl N-α-Methyl-L-Phenylalanine hydrochloride;N-Methylphenylalanine hydrochloride
• CAS NO: 66866-67-9
• Molecular Formula: C₁₀H₁₃NO₂*ClH
• Molecular Weight: 215.68
• Product Categories: N-Methyl Amino Acids;Peptide Synthesis;Unnatural Amino Acid Derivatives
• Mol File: 66866-67-9.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• BRN: 4018032
• CAS DataBase Reference: N-METHYL-L-PHENYLALANINE HYDROCHLORIDE(CAS DataBase Reference)
• NIST Chemistry Reference: N-METHYL-L-PHENYLALANINE HYDROCHLORIDE(66866-67-9)
• EPA Substance Registry System: N-METHYL-L-PHENYLALANINE HYDROCHLORIDE(66866-67-9)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 66866-67-9(Hazardous Substances Data)

Usage

General Description

N-Methyl-L-phenylalanine hydrochloride is a chemical compound commonly used in research and pharmaceutical applications. It is a derivative of the amino acid L-phenylalanine, with an added methyl group. N-METHYL-L-PHENYLALANINE HYDROCHLORIDE is often used in the synthesis of peptides and proteins, as well as in the development of pharmaceutical drugs. It is a white crystalline powder that is soluble in water, and it has been studied for its potential therapeutic effects on conditions such as depression and chronic pain. N-Methyl-L-phenylalanine hydrochloride is considered a valuable building block in medicinal chemistry due to its versatile use in drug development and biological research.

Upstream product

• 914606-75-0 micropeptin MZ₈₄₅ 
• 1207348-70-6 micropeptin MZ₈₅₉ 
• 1207348-72-8 micropeptin MZ₉₃₉A 
• 1207348-74-0 micropeptin MZ₉₂₅ 
• 1207348-76-2 micropeptin MZ₉₃₉B 
• 1207348-78-4 micropeptin MZ₁₀₁₉ 
• 1207348-80-8 micropeptin MZ₇₇₁ 
• 3081-24-1 H-Phe-OEt 
• 159090-55-8 N-Boc-N-methyl-L-phenylalanine ethyl ester 
• 67-56-1 methanol 
• 37553-65-4 Boc-N-Me-Phe-OH 

Downstream Products

• 76370-06-4 N-Boc-(N-Me)Phe-(N-Me)Phe-OMe 
• 94779-19-8 N-Boc-Pro-Phe-(N-Me)Phe-OMe 
• 1471519-98-8 N-Boc-Tyr-Pro-Phe-(N-Me)Phe-OMe 
• 1471520-08-7 N-Boc-Tyr-Pro-Phe-(N-Me)Phe-NH(CH₂)₂OH 
• 1471520-19-0 TFA·Tyr-Pro-Phe-(N-Me)Phe-NH(CH₂)₂OH 
• 1471519-96-6 N-Boc-Pro-(N-Me)Phe-(N-Me)Phe-OMe 
• 1471520-06-5 N-Boc-Tyr-Pro-(N-Me)Phe-(N-Me)Phe-OMe 
• 1471520-16-7 N-Boc-Tyr-Pro-(N-Me)Phe-(N-Me)Phe-NH(CH₂)₂OH 
• 1471520-31-6 TFA·Tyr-Pro-(N-Me)Phe-(N-Me)Phe-NH(CH₂)₂OH 
• 94779-17-6 N-Boc-Phe-(N-Me)Phe-OMe 
• 77128-73-5 (2S)-N-fluorenylmethyloxycarbonyl-2-amino-N-methyl-3-phenylpropanoic acid 

Relevant articles and documents

Hybrid peptides endomophin-2/DAMGO: Design, synthesis and biological evaluation

Endomorphin-2 [Tyr-Pro-Phe-Phe-NH2] and DAMGO [Tyr-D-Ala-Gly-(N-Me)Phe-Gly-ol] are natural (EM2) and synthetic (DAMGO) opioid peptides both selective for μ opioid receptor with high analgesic activity. In this work we report synthesis, in vitro and in vivo biological evaluation of five new hybrid EM2/DAMGO analogues, with the aim to obtain compounds with high affinity at μ-opioid receptor, high activity in animal nociception tests (hot plate and tail flick) and improved enzymatic stability. Double N-methylation on both Phe residues and C-terminal ethanolamide led to analogue 6e, which possesses a good in vitro μ affinity (Kiμ = 34 nM), combined with a remarkable in vivo antinociceptive activity.

Micropeptins from an Israeli fishpond water bloom of the cyanobacterium microcystis sp

Seven new natural products, micropeptin MZ845 (1), micropeptin MZ859 (2), micropeptin MZ939A (3), micropeptin MZ925 (4), micropeptin MZ939B (5), micropeptin MZ1019 (6), and micropeptin MZ771 (7), as well as two known micropeptins, cyanopeptolin S (8) and cyanopeptolin SS (9), were isolated from the hydrophilic extract of the cyanobacterium Microcystis sp. that was collected from a fishpond in Kibbutz Ma'ayan Tzvi, Israel, in July 2006. The structures of the pure natural products were elucidated using spectroscopic methods, including UV, 1D and 2D NMR, and MS techniques. The absolute configuration of the chiral centers of the compounds was determined using Marfey's method for HPLC. The inhibitory activity of the compounds was determined for the serine proteases: trypsin, chymotrypsin, thrombin, and elastase. These micropeptins inhibited trypsin with IC50's that varied between 0.6 and 24.2 μM. The SAR of these micropeptins is discussed.