27513-48-0

Upstream product

• 3978-80-1 Boc-Tyr-OH 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 24424-99-5 di-tert-butyl dicarbonate 
• 60-18-4 L-tyrosine 
• 1080-06-4 L-Tyr-OMe 
• 175214-20-7 Cbz-Tyr(MPM)-OMe 
• 175214-21-8 Tyr(MPM)-OMe 
• 13512-31-7 N-(benzyloxycarbonyl)-L-tyrosine methyl ester 
• 1164-16-5 Z-L-Tyr-OH 
• 187328-92-3 Boc-Tyr(Bn)-Tyr(MPM)-OMe 

Downstream Products

• 881887-95-2 N^α-(tert-butoxycarbonyl)-L-tyrosyl-L-tyrosine 
• 1373311-94-4 C₃₂H₂₉IN₂O₄ 
• 1373311-92-2 (3S,6S)-3,6-bis(4-(benzyloxy)-3-iodobenzyl)piperazine-2,5-dione 
• 1373311-93-3 (4²S,4⁵S)-1⁶,2⁶-bis(benzyloxy)-4(2,5)-piperazina-1,2(1,3)-dibenzenacyclopentaphane-4³,46-dione 
• 374674-80-3 (3S,6S)-3,6-bis(p-(benzyloxy)benzyl)piperazine-2,5-dione 
• 10125-11-8 cis-3,6-bis(4-hydroxybenzyl)piperazine-2,5-dione 

Relevant academic research and scientific papers

A novel molecular scaffold resensitizes multidrug-resistant S. aureus to fluoroquinolones

Nosocomial infections arising from opportunistic pathogens, such as Staphylococcus aureus, are growing unabated, compounded by the rapid emergence of antimicrobial resistance. Herein, we demonstrate a new molecular design that exhibits excellent activity against multidrug-resistant S. aureus with no cytotoxicity and resensitizes fluoroquinolones (FQ) towards FQ-resistant methicillin-resistant S. aureus strains, with DNA gyrase B as the likely molecular target as determined by molecular dynamics (MD) simulations.

Structure-Activity Relationships of cyclo(l -Tyrosyl- l -tyrosine) Derivatives Binding to Mycobacterium tuberculosis CYP121: Iodinated Analogues Promote Shift to High-Spin Adduct

A series of analogues of cyclo(l-tyrosyl-l-tyrosine), the substrate of the Mycobacterium tuberculosis enzyme CYP121, have been synthesized and analyzed by UV-vis and electron paramagnetic resonance spectroscopy and by X-ray crystallography. The introduction of iodine substituents onto cyclo(l-tyrosyl-l-tyrosine) results in sub-μM binding affinity for the CYP121 enzyme and a complete shift to the high-spin state of the heme FeIII. The introduction of halogens that are able to interact with heme groups is thus a feasible approach to the development of next-generation, tight binding inhibitors of the CYP121 enzyme, in the search for novel antitubercular compounds.

Total Synthesis of Herquline B and C

The total syntheses of (-)-herquline B (2) and a heretofore-unrecognized congener, (+)-herquline C (3), are described. The syntheses require 14 and 13 steps, respectively, and feature a key oxazoline reduction that sets the stage for piperazine construction.

Sulfotyrosine dipeptide: Synthesis and evaluation as HIV-entry inhibitor

Human immunodeficiency virus type 1 (HIV-1) is responsible for the worldwide AIDS pandemic. Due to the lack of prophylactic HIV-1 vaccine, drug treatment of the infected patients becomes essential to reduce the viral load and to slow down progression of the disease. Because of drug resistance, finding new antiviral agents is necessary for AIDS drug therapies. The interaction of gp120 and co-receptor (CCR5/CXCR4) mediates the entry of HIV-1 into host cells, which has been increasingly exploited in recent years as the target for new antiviral agents. A conserved co-receptor binding site on gp120 that recognizes sulfotyrosine (sTyr) residues represents a structural target to design novel HIV entry inhibitors. In this work, we developed an efficient synthesis of sulfotyrosine dipeptide and evaluated it as an HIV-1 entry inhibitor.

Total synthesis of mycocyclosin

The first total synthesis of mycocyclosin, a diketopiperazine natural product isolated from M. tuberculosis, is described. While direct oxidative coupling of tyrosine phenolic groups was unsuccessful, construction of the highly strained bicyclic framework was successfully accomplished through an intramolecular Miyaura-Suzuki cross-coupling to generate the biaryl linkage.

Ditryptophan conjugation triggers conversion of biotin fibers into soft spherical structures

(Figure Presented) Trigger happy: Biotin and its methyl ester form long fibers in solution, which are transformed into soft spherical structures upon simple conjugation with ditryptophan dipeptide (see picture). Such morphogenesis is not achieved in a controlled fashion by other aromatic amino acids.

A mechanistic and kinetic study of the formation of metal nanoparticles by using synthetic tyrosine-based oligopeptides

Synthetic oligopeptides containing redox-active tyrosine residues have been employed to prepare gold and silver nanoparticles. In this reduction process an electron from the tyrosinate ion of the peptide is transferred to the metal ion at basic pH through the formation of a tyrosyl radical, which is eventually converted to its dityrosine form during the reaction. This reaction mechanism was confirmed from UV-visible, fluorescence, and EPR spectroscopy and was found to be pH-dependent. Transmission electron microscopy measurement shows that the average size and the monodispersity of gold nanoparticles increase as the number of tyrosine residues in the peptide increases. The kinetic study, based on spectrophotometric measurements of the surface plasmon resonance optical property, shows that the rate of formation of gold nanoparticles was much faster at higher pH than at lower pH and was also dependent on the number of tyrosine residues present in the peptide. The dityrosine form of the peptide was found to retain reducing properties like those of tyrosine in basic medium.

Smart oligopeptide gels: In situ formation and stabilization of gold and silver nanoparticles within supramolecular organogel networks

Tripeptide with redox active chemical entities based smart organogels have been used for in situ formation and stabilization of gold and silver nanoparticles within the supramolecular gel networks and the gold nanoparticles are aligned in arrays along the gel nanofibers of peptide 1-toluene gels. The Royal Society of Chemistry 2006.

Interaction between quaternary ammonium ions and dipeptides: Positive anion allosteric effect

The binding properties of dipeptides possessing aromatic residues towards quaternary ammonium ions have been investigated by 1H-NMR spectroscopy. The intermolecular hydrogen bonding between exchangeable protons (OH and NH) of aromatic residues

Pd/C-catalyzed chemoselective hydrogenation in the presence of a phenolic MPM protective group using pyridine as a catalyst poison

Employment of a Pd/C-pyridine combination as a catalyst is a very useful method for the selective removal (hydrogenolysis) of phenolic O-benzyl, N-Cbz and benzyl ester protective groups and for the selective hydrogenation of nitro and olefin functions of phenol derivatives protected with the MPM group. These discriminatory results are apparently attributable to the effect of pyridine. The MPM group could be extensively applied to chemoselective hydrogenation as a protective group for phenolic hydroxyl functions.