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Usage

Uses

Used in Pharmaceutical Development:
N-METHYL-L-PHENYLALANINE HYDROCHLORIDE is used as an active pharmaceutical ingredient for the development of drugs targeting various medical conditions. Its potential therapeutic effects on depression and chronic pain highlight its importance in creating novel treatments for these conditions.
Used in Peptide and Protein Synthesis:
In the field of biochemistry, N-METHYL-L-PHENYLALANINE HYDROCHLORIDE is used as a building block for the synthesis of peptides and proteins. Its incorporation into these biological molecules allows for the exploration of new protein functions and the development of bioactive compounds.
Used in Research Applications:
N-METHYL-L-PHENYLALANINE HYDROCHLORIDE is used as a research tool in laboratories for studying the structure and function of proteins, as well as for investigating the mechanisms of various diseases. Its versatility in research contributes to a deeper understanding of biological processes and the discovery of new therapeutic targets.
Used in Medicinal Chemistry:
In the industry of medicinal chemistry, N-METHYL-L-PHENYLALANINE HYDROCHLORIDE is used as a key component in the design and synthesis of new drugs. Its unique properties and reactivity make it an essential part of the drug discovery process, aiding in the creation of innovative pharmaceuticals to address unmet medical needs.

Upstream product

• 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 
• 1207348-78-4 micropeptin MZ₁₀₁₉ 
• 1207348-76-2 micropeptin MZ₉₃₉B 
• 1207348-74-0 micropeptin MZ₉₂₅ 
• 1207348-72-8 micropeptin MZ₉₃₉A 
• 1207348-70-6 micropeptin MZ₈₅₉ 
• 914606-75-0 micropeptin MZ₈₄₅ 

Downstream Products

• 2439-60-3 N-methyl-L-phenylalanine methyl ester 
• 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 

Relevant academic research and scientific papers

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.

Symplocin A, a linear peptide from the bahamian cyanobacterium symploca sp. configurational analysis of N, N -dimethylamino acids by chiral-phase HPLC of naphthacyl esters

The absolute stereostructures of the components of symplocin A (3), a new N,N-dimethyl-terminated peptide from the Bahamian cyanobacterium Symploca sp., were assigned from spectroscopic analysis, including MS, 2D NMR, and Marfey's analysis. The complete a

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.