56564-52-4

Usage

Uses

Used in Pharmaceutical Industry:
H-D-MEPHE-OH HCL is used as a key component in the preparation of phosphate/sulfate ester compounds and their pharmaceutical compositions. These compounds are specifically designed for the inhibition of protein interacting NIMA (PIN 1), a peptidyl-prolyl isomerase enzyme that plays a crucial role in various cellular processes, including cell cycle regulation, signal transduction, and protein folding.
The inhibition of PIN 1 has been implicated in the regulation of various diseases, such as cancer, neurodegenerative disorders, and viral infections. By targeting PIN 1, H-D-MEPHE-OH HCL-based pharmaceutical compositions can potentially offer novel therapeutic strategies for the treatment of these conditions.
Furthermore, the use of H-D-MEPHE-OH HCL in the development of pharmaceutical compositions allows for the exploration of its potential synergistic effects with other drugs or compounds, enhancing the overall efficacy of treatment regimens. This opens up new avenues for research and development in the pharmaceutical industry, paving the way for innovative and effective therapeutic solutions.

InChI:InChI=1/C10H13NO2/c1-11-9(10(12)13)7-8-5-3-2-4-6-8/h2-6,9,11H,7H2,1H3,(H,12,13)/t9-/m1/s1

Upstream product

• 7474-06-8 (S)-2-chloro-3-phenyl-propionic acid 
• 74-89-5 methylamine 
• 93529-74-9 (S)-N-(4-chlorobenzylidene)phenylalanine methyl ester 
• 77-78-1 dimethyl sulfate 
• 93473-37-1 (S)-2-(Dimethylamino-methyleneamino)-3-phenyl-propionic acid methyl ester 
• 30634-71-0 C₁₄H₂₀N₂O₂ 
• 333-27-7 methyl trifluoromethanesulfonate 
• 170642-33-8 (S,S)-pseudoephedrine N-methyl-D-phenylalaninamide 
• 7647-01-0 hydrogenchloride 
• 124312-54-5 2-(N,4-dimethylphenylsulfonamido)-3-phenylpropanoic acid 
• 64-19-7 acetic acid 
• 10034-85-2 hydrogen iodide 
• 172721-98-1 (3R, 6R)-4-methyl-6-(1-methylethyl)-3-phenylmethylperhydro-1,4-oxazine-2,5-dione 
• 114526-00-0 (2R)-2-[[(benzyloxy)carbonyl](methyl)amino]-3-phenylpropanoic acid 

Downstream Products

• 19881-54-0 N-methyl-D-phenylalanine ethyl ester; hydrochloride 
• 130008-09-2 methyl N-methyl-D-phenylalaninate hydrochloride 
• 114525-95-0 (R)-tert-butyl 2-(methylamino)-3-phenylpropanoate 
• 102339-81-1 (2R)-2-(Methylamino)-3-phenylpropan-1-ol 
• 1309656-45-8 C₂₀H₂₇N₂O₄P 
• 194736-83-9 D-N-Me-Phe-FDAA 
• 1571105-51-5 C₆₀H₉₄N₁₂O₁₀ 
• 1571105-54-8 C₅₈H₉₀N₁₂O₁₀ 
• 1571105-48-0 C₆₁H₉₄N₁₂O₁₀ 

Relevant academic research and scientific papers

Isolation, Structure Determination, and Total Synthesis of Hoshinoamide C, an Antiparasitic Lipopeptide from the Marine Cyanobacterium Caldora penicillata

Hoshinoamide C (1), an antiparasitic lipopeptide, was isolated from the marine cyanobacterium Caldora penicillata. Its planar structure was elucidated by spectral analyses, mainly 2D NMR, and the absolute configurations of the α-amino acid moieties were determined by degradation reactions followed by chiral-phase HPLC analyses. To clarify the absolute configuration of an unusual amino acid moiety, we synthesized two possible diastereomers of hoshinoamide C and determined its absolute configuration based on a comparison of their spectroscopic data with those of the natural compound. Hoshinoamide C (1) did not exhibit any cytotoxicity against HeLa or HL60 cells at 10 μM, but inhibited the growth of the parasites responsible for malaria (IC50 0.96 μM) and African sleeping sickness (IC50 2.9 μM).

Isolation and Total Synthesis of Mabuniamide, a Lipopeptide from an Okeania sp. Marine Cyanobacterium

The bioassay-guided fractionation of an Okeania sp. marine cyanobacterium collected in Okinawa led to the isolation of the lipopeptide mabuniamide (1). The gross structure of 1 was determined by spectroscopic analyses, and its absolute configuration was determined using Marfey's analysis of the acid hydrolysate of 1. The absolute configuration of 1 was confirmed by total synthesis. Mabuniamide (1) stimulated glucose uptake in cultured rat L6 myotubes. In addition, mabuniamide (1) and its stereoisomer (2) exhibited moderate antimalarial activity.

Isolation, structure elucidation and biological evaluation of lagunamide D: A new cytotoxic macrocyclic depsipeptide from marine cyanobacteria

Lagunamide D, a new cytotoxic macrocyclic depsipeptide, was discovered from a collection of marine cyanobacteria from Loggerhead Key in the Dry Tortugas, Florida. An intramolecular ester exchange was observed, where the 26-membered macrocycle could contract to a 24-membered compound via acyl migration at the 1,3-diol unit, and the transformation product was named lagunamide D'. The planar structures of both compounds were elucidated using a combination of nuclear magnetic resonance (NMR) spectroscopy and high-resolution mass spectroscopy (HRMS). The absolute configurations were determined on the basis of enantioselective analysis, modified Mosher's analysis, Kishi NMR database, and direct comparison with lagunamide A, a structure closely resembling lagunamide D. Lagunamides A and D displayed low-nanomolar antiproliferative activity against A549 human lung adenocarcinoma cells, while the structural transformation from the 26-membered lagunamide D macrocycle to the 24-membered ring structure for lagunamide D' led to a 9.6-fold decrease in activity. Lagunamide D also displayed potent activity in triggering apoptosis in a dose- and time-dependent manner. Further investigation on the mechanism of action of the lagunamide scaffold is needed to fully explore its therapeutic potential as an anticancer agent.

Discovery of Amantamide, a Selective CXCR7 Agonist from Marine Cyanobacteria

CXCR7 plays an emerging role in several physiological processes. A linear peptide, amantamide (1), was isolated from marine cyanobacteria, and the structure was determined by NMR and mass spectrometry. The total synthesis was achieved by solid-phase method. After screening two biological target libraries, 1 was identified as a selective CXCR7 agonist. The selective activation of CXCR7 by 1 could provide the basis for developing CXCR7-targeted therapeutics and deciphering the role of CXCR7 in different diseases.

Odoamide, a cytotoxic cyclodepsipeptide from the marine cyanobacterium Okeania sp.

The bioassay-guided fractionation of the Okinawan marine cyanobacterium Okeania sp. led to the isolation of the 26-membered cyclodepsipeptide odoamide (1). The gross structure of 1 was determined by 1D and 2D NMR analyses, whereas its absolute stereochemistry was determined using a variety of different methods, including synthesis and chemical degradation followed by chiral HPLC analysis. Notably, odoamide (1) showed potent cytotoxicity against HeLa S3 human cervical cancer cells with an IC50value of 26.3?nM.

Ulleungamides A and B, Modified α,β-Dehydropipecolic Acid Containing Cyclic Depsipeptides from Streptomyces sp. KCB13F003

Two novel cyclic depsipeptides, ulleungamides A (1) and B (2), were isolated from cultures of terrestrial Streptomyces sp. Their structures were determined by analyses of spectroscopic data and various chemical transformations, including modified Mosher's method, advanced Marfey's method, PGME, GITC derivatizations, and Snatzke's method. Ulleungamides were determined to be a new class of peptides bearing unprecedented units, such as 5-hydroxy-6-methyl-2,3-dehydropipecolic acid, 4,5-dihydroxy-6-methyl-2,3-dehydropipecolic acid, and amino-linked 2-isopropylsuccinic acid. Ulleungamide A displayed growth inhibitory activity against Staphylococcus aureus and Salmonella typhimurium without cytotoxicity.

Maedamide, a novel chymotrypsin inhibitor from a marine cyanobacterial assemblage of Lyngbya sp.

Maedamide, a novel chymotrypsin-inhibiting depsipeptide, was isolated from a cyanobacterial assemblage that mostly consisted of Lyngbya sp. Its structure was elucidated by spectroscopic analyses and chiral HPLC analyses of hydrolysis products. Maedamide selectively inhibited chymotrypsin but not elastase and trypsin. In addition, Maedamide strongly inhibited the growth of HeLa cells and HL60 cells.

Maedamide, a novel chymotrypsin inhibitor from a marine cyanobacterial assemblage of Lyngbya sp.

Maedamide, a novel chymotrypsin-inhibiting depsipeptide, was isolated from a cyanobacterial assemblage that mostly consisted of Lyngbya sp. Its structure was elucidated by spectroscopic analyses and chiral HPLC analyses of hydrolysis products. Maedamide selectively inhibited chymotrypsin but not elastase and trypsin. In addition, Maedamide strongly inhibited the growth of HeLa cells and HL60 cells.

Lipopeptides from the tropical marine cyanobacterium symploca sp.

A collection of the tropical marine cyanobacterium Symploca sp., collected near Kimbe Bay, Papua New Guinea, previously yielded several new metabolites including kimbeamides A-C, kimbelactone A, and tasihalide C. Investigations into a more polar cytotoxic fraction yielded three new lipopeptides, tasiamides C-E (1-3). The planar structures were deduced by 2D NMR spectroscopy and tandem mass spectrometry, and their absolute configurations were determined by a combination of Marfeys and chiral-phase GC-MS analysis. These new metabolites are similar to several previously isolated compounds, including tasiamide (4), grassystatins (5, 6), and symplocin A, all of which were isolated from similar filamentous marine cyanobacteria.

Isolation of ciliatamide D from a marine sponge Stelletta sp. and a reinvestigation of the configuration of ciliatamide A

A new lipopeptide, ciliatamide D (1), was isolated from a marine sponge Stelletta sp., collected at Oshimashinsone, together with the known compound ciliatamide A (2). Ciliatamide D (1) is a congener of 2, in which N-Me-Phe is replaced by N-Me-Met(O). Marfey's analysis of the acid hydrolysate of 1 demonstrated that the two constituent amino acids were both in the l-form. This result prompted us to carefully investigate the configuration of 2, resulting in the assignment of the l-form for both residues.