L-Phenylalanine tert-butyl ester hydrochloride
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L-Phenylalanine tert-butyl ester hydrochloride

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L-Amino Acids
Catalog number
CAS number
Molecular Formula
Molecular Weight
L-Phenylalanine tert-butyl ester hydrochloride
tert-butyl (2S)-2-amino-3-phenylpropanoate;hydrochloride
L-Phe-OtBu HCl; tert-Butyl 3-phenyl-L-alaninate hydrochloride; L-Phenylalnine t-Butyl Ester Hydrochloride; H-Phe-OtBu HCl
White crystalline powder
≥ 99% (HPLC)
Melting Point
235 °C
Boiling Point
303.3 °C at 760 mmHg
Store at 2-8 °C
InChI Key
Canonical SMILES
1. Tyrosine nitration, dimerization, and hydroxylation by peroxynitrite in membranes as studied by the hydrophobic probe N-t-BOC-l-tyrosine tert-butyl ester
Silvina Bartesaghi, Gonzalo Peluffo, Hao Zhang, Joy Joseph, Balaraman Kalyanaraman, Rafael Radi Methods Enzymol. 2008;441:217-36. doi: 10.1016/S0076-6879(08)01212-3.
Protein tyrosine oxidation mechanisms in hydrophobic biocompartments (i.e., biomembranes, lipoproteins) leading to nitrated, dimerized, and hydroxylated products are just starting to be appreciated. This chapter reports on the use of the hydrophobic tyrosine analog N-t-BOC-l-tyrosine tert-butyl ester (BTBE) incorporated to phosphatidyl choline liposomes to study peroxynitrite-dependent tyrosine oxidation processes in model biomembranes. The probe proved to be valuable in defining the role of biologically relevant variables in the oxidation process, including the action of hydrophilic and hydrophobic peroxynitrite and peroxynitrite-derived free radical scavengers, transition metal catalysts, carbon dioxide, molecular oxygen, pH, and fatty acid unsaturation degree. Moreover, detection of the BTBE phenoxyl radical and relative product distribution yields of 3-nitro-, 3,3'-di-, and 3-hydroxy-BTBE in the membrane fully accommodate with a free radical mechanism of tyrosine oxidation, with physical chemical and biochemical determinants that in several respects differ of those participating in aqueous environments. The methods presented herein can be extended to explore the reaction mechanisms of tyrosine oxidation by other biologically relevant oxidants and in other hydrophobic biocompartments.
2. Mechanistic studies of peroxynitrite-mediated tyrosine nitration in membranes using the hydrophobic probe N-t-BOC-L-tyrosine tert-butyl ester
Silvina Bartesaghi, Valeria Valez, Madia Trujillo, Gonzalo Peluffo, Natalia Romero, Hao Zhang, Balaraman Kalyanaraman, Rafael Radi Biochemistry. 2006 Jun 6;45(22):6813-25. doi: 10.1021/bi060363x.
Most of the mechanistic studies of tyrosine nitration have been performed in aqueous solution. However, many protein tyrosine residues shown to be nitrated in vitro and in vivo are associated to nonpolar compartments. In this work, we have used the stable hydrophobic tyrosine analogue N-t-BOC-L-tyrosine tert-butyl ester (BTBE) incorporated into phosphatidylcholine (PC) liposomes to study physicochemical and biochemical factors that control peroxynitrite-dependent tyrosine nitration in phospholipid bilayers. Peroxynitrite leads to maximum 3-nitro-BTBE yields (3%) at pH 7.4. In addition, small amounts of 3,3'-di-BTBE were formed at pH 7.4 (0.02%) which increased over alkaline pH; at pH 6, a hydroxylated derivative of BTBE was identified by HPLC-MS analysis. BTBE nitration yields were similar in dilauroyl- and dimyristoyl-PC and were also significant in the polyunsaturated fatty acid-containing egg PC. *OH and *NO2 scavengers inhibited BTBE nitration. In contrast to tyrosine in the aqueous phase, the presence of CO2 decreased BTBE nitration, indicating that CO3*- cannot permeate to the compartment where BTBE is located. On the other hand, micromolar concentrations of hemin and Mn-tccp strongly enhanced BTBE nitration. Electron spin resonance (ESR) detection of the BTBE phenoxyl radical and kinetic modeling of the pH profiles of BTBE nitration and dimerization were in full agreement with a free radical mechanism of oxidation initiated by ONOOH homolysis in the immediacy of or even inside the bilayer and with a diffusion coefficient of BTBE phenoxyl radical 100 times less than for the aqueous phase tyrosyl radical. BTBE was successfully applied as a hydrophobic probe to study nitration mechanisms and will serve to study factors controlling protein and lipid nitration in biomembranes and lipoproteins.
3. Incorporation of the hydrophobic probe N-t-BOC-L-tyrosine tert-butyl ester to red blood cell membranes to study peroxynitrite-dependent reactions
Natalia Romero, Gonzalo Peluffo, Silvina Bartesaghi, Hao Zhang, Joy Joseph, Balaraman Kalyanaraman, Rafael Radi Chem Res Toxicol. 2007 Nov;20(11):1638-48. doi: 10.1021/tx700142a. Epub 2007 Oct 18.
We have previously demonstrated that red blood cells (RBC) are an important sink of intravascularly generated peroxynitrite even in the presence of physiological concentrations of CO2 or other plasmatic biotargets. Once inside erythrocytes, peroxynitrite reacts fast with oxyhemoglobin (oxyHb; k2=2 x 10(4) M(-1) s(-1) at 37 degrees C and pH 7.4) and isomerizes to nitrate. Herein, we investigated whether, in spite of the fast diffusion and consumption of extracellularly added peroxynitrite by intraerythrocytic oxyHb, peroxynitrite-dependent radical processes could occur at the RBC membrane, focusing on tyrosine nitration. For this purpose, the hydrophobic tyrosine analogue N-t-BOC-L-tyrosine tert-butyl ester (BTBE) was successfully incorporated for the first time to a biological membrane, that is, RBC membrane, with incorporation yields approximately 1-3 x 10(7) molecules per RBC. The membrane integrity of BTBE-containing RBC was not significantly altered after BTBE incorporation as demonstrated by permeability studies. The probe was then used to study peroxynitrite-dependent reactions. The addition of peroxynitrite to BTBE-containing RBC suspensions resulted in BTBE nitration and dimerization to 3-nitro-BTBE and 3,3'-di-BTBE, respectively, indicative of peroxynitrite-derived radicals reactions in the membrane. Peroxynitrite addition to RBC also caused tyrosine nitration of membrane-associated proteins. The free radical nature of the process was also shown by the detection of protein-derived radicals by DMPO-immunospin trapping. While the presence of extracellular CO2 was potently inhibitory of intracellular oxyHb oxidation, membrane protein and BTBE nitration by peroxynitrite at
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