18875-48-4Relevant articles and documents
Detection of Localized Hepatocellular Amino Acid Kinetics by using Mass Spectrometry Imaging of Stable Isotopes
Arts, Martijn,Soons, Zita,Ellis, Shane R.,Pierzchalski, Keely A.,Balluff, Benjamin,Eijkel, Gert B.,Dubois, Ludwig J.,Lieuwes, Natasja G.,Agten, Stijn M.,Hackeng, Tilman M.,van Loon, Luc J. C.,Heeren, Ron M. A.,Olde Damink, Steven W. M.
, p. 7146 - 7150 (2017)
Mass spectrometry imaging (MSI) simultaneously detects and identifies the spatial distribution of numerous molecules throughout tissues. Currently, MSI is limited to providing a static and ex vivo snapshot of highly dynamic systems in which molecules are constantly synthesized and consumed. Herein, we demonstrate an innovative MSI methodology to study dynamic molecular changes of amino acids within biological tissues by measuring the dilution and conversion of stable isotopes in a mouse model. We evaluate the method specifically on hepatocellular metabolism of the essential amino acid l-phenylalanine, associated with liver diseases. Crucially, the method reveals the localized dynamics of l-phenylalanine metabolism, including its in vivo hydroxylation to l-tyrosine and co-localization with other liver metabolites in a time course of samples from different animals. This method thus enables the dynamics of localized biochemical synthesis to be studied directly from biological tissues.
Formation of m-tyrosine and o-tyrosine from L-phenylalanine in various tissues of rats.
Ishimitsu,Fujimoto,Ohara
, p. 3887 - 3892 (1985)
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Kinetic of adsorption and of photocatalytic degradation of phenylalanine effect of pH and light intensity
Elsellami,Vocanson,Dappozze,Puzenat,Pa?sse,Houas,Guillard
, p. 142 - 148 (2010)
Phenylalanine (Phe) was chosen to study the TiO2 photocatalytic degradation of amino acids, which are at the origin of the formation of odorous compounds after chlorination. The photocatalytic degradation has been investigated in aqueous solutions containing TiO2 suspensions as photocatalyst, in order to assess the influence of various parameters, such as adsorption, initial concentration, pH and radiant flux on the photocatalytic process. Results showed no correlation between dark adsorption and photocatalytic degradation. A multilayer kinetic was observed in the dark with a monolayer corresponding to less that 1% of OH covered, whereas Langmuir-Hinshelwood model seems to modelize the photocatalytic disappearance of Phe. However, even if the form of the curve is similar to L-H model, the degradation of phenylalanine is not a kinetic of L-H as we could plan it by considering the adsorption of the phenylalanine in the dark. The study of the mineralization of carbon and nitrogen showed that nitrogen atoms were predominantly photoconverted into NH4+ and a total mineralization of nitrogen and carbon seems occur. The identification of the by-products by LC-MS reveal mono- and di-hydroxylation and nitrogen-carbon (N-C) cleavage. The effect of pH showed an increase of adsorption under acid pH but a decrease of disappearance rate. The more efficient degradation was found at basic pH. The evolution of hydroxylated compounds of phenylalanine as a function of conversion revealed the presence of more hydroxylated compounds at natural pH and at basic pH compared to acid pH suggesting a modification of mechanism with solution pH. The effect of the radiant flux evaluated under different initial concentration of phenylalanine allowed us to determine that Κ increases by increasing the radiant flux, whereas Κ decreases or remains constant from about a value of 3.5 mW/cm2. The disappearance rate as a function of radiant flux has been showed to reach a maximal value corresponding to a maximal quantum yield of 1.6%.
The photochemical decomposition and hydroxylation of phenylalanine in the presence of riboflavin.
Ishimitsu,Fujimoto,Ohara
, p. 1552 - 1556 (1985)
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Studies on the formation of 3,4-dihydroxyphenylalanine, m-tyrosine and o-tyrosine from L-phenylalanine by rat liver and adrenal
Ishimitsu,Fujimoto,Ohara
, p. 279 - 285 (1988)
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Hydroxylation of Phenylalanine by Aqueous H2O2 in the Presence of an Artificial Water-soluble Iron Porphyrin Complex
Shimidzu, Takeo,Iyoda, Tomokazu,Kanda, Naoya
, p. 1206 - 1207 (1981)
Phenylalanine is hydroxylated by aqueous H2O2 in the presence of a catalytic amount of an artificial water-soluble iron porphyrin complex (1) to give monohydroxylated and dihydroxylated products, i.e., tyrosine and dihydroxyphenylalanine, which are obtained in good yields.
Enzymatic Reactions in Aqueous-Organic media. XVII. Optical Resolution of Amino Acid Esters by Enzymatic Hydrolysis in Organic Solvents
Tomiuchi, Yoshimasa,Ohshima, Kouji,Kise, Hideo
, p. 2599 - 2603 (1992)
Enantiospecific hydrolysis of DL-tyrosine ethyl ester was carried out using α-chymotrypsin (CT) as a catalyst in organic solvents, and L-tyrosine was obtained with high optical purity.Activity and enantiospecificity of CT were found to be greatly altered by water content in the reaction media, and generally high enantiospecificity was observed at low water contents.Many of natural and unnatural amino acid esters were resolved by hydrolysis in organic solvents using CT, subtilisin Carlsberg, or subtilisin BPN' as catalysts.
L-tyrosine β-naphthylamide is a potent competitive inhibitor of tyramine n-(hydroxycinnamoyl)transferase in vitro
Negrel, Jonathan,Javelle, Francine
, p. 523 - 527 (2001)
L-Tyrosine β-naphthylamide, a synthetic substrate designed to measure tyrosine aminopeptidase activity, is a potent inhibitor of hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase (THT) purified from elicited tobacco cell-suspension cultures. T
Enantioselective reductive amination of α-keto acids to α-amino acids by a pyridoxamine cofactor in a protein cavity
Kuang, Hao,Brown, Matthew L.,Davies, Ronald R.,Young, Eva C.,Distefano, Mark D.
, p. 10702 - 10706 (1996)
Adipocyte lipid binding protein (ALBP) is a small 131 residue protein with a simple architecture that consists of two orthogonal planes of β-sheet secondary structure. This protein binds a variety of fatty acids in a large cavity formed between the two sheets such that the bound ligands are completely enclosed within the protein. In this paper, the synthesis of an ALBP conjugate (ALBP-PX) containing a pyridoxamine cofactor attached to a thiol within the protein interior is described. The conjugate was characterized by mass spectrometry, UV/vis spectroscopy, and gel filtration chromatography. ALBP-PX reductively aminates a number of alkyl, aryl, and side chain functionalized α-keto acids to α-amino acids with enantioselectivities as high as 94% ee.
Anti-inflammatory amino acid derivatives from the ascidian Herdmania momus
Li, Jian Lin,Han, Sang Chul,Yoo, Eun Sook,Shin, Sook,Hong, Jongki,Cui, Zheng,Li, Huayue,Jung, Jee H.
, p. 1792 - 1797 (2011)
Four new amino acid derivatives, herdmanines A-D (1-4), were isolated from the marine ascidian Herdmania momus. Herdmanines A-C contain the unusual d-form of arginine. Compounds 3 and 4 had a moderate suppressive effect on the production of NO, with IC50 values of 96 and 9 μM, respectively. These compounds were found to inhibit the mRNA expression of iNOS. The inhibitory activities on the production and mRNA expression of pro-inflammatory cytokines such as TNF-α, IL-1β, and IL-6 were evaluated.
Free-radical Formation in the Pulse-radiolysis Oxidation of Inactive Escherichia coli Met-R2 Ribonucleotide Reductase
Lam, Kin-Yu,Govindaraju, K.,Han, Joo-Yeon,Salmon, G. Arthur,Sykes, A. Geoffrey
, p. 2797 - 2802 (1993)
The regeneration of a tyrosyl radical from the inactive Escherichia coli met-R2 enzyme using pulse radiolytically generated azide radicals N3(.) has been studied.Tryptophan and tyrosine amino acid residues on the protein are reactive towards N3(.) with the formation of either a tryptophan radical (peak at 510 nm) or a tyrosyl radical (peak at 410 nm).The combined rate constant (19 deg C) obtained for the formation of both these deprotonated species in N2O-saturated solution, = 0.012 M, pH 7 (40 mM phosphate), and I = 0.100 M, is 1.75 x 1E9 M-1 s-1.Biphasic decay of the tryptophan radical is then observed, rate constants 2.9 x 1E3 and 7.3 x 1E2 s-1, which are assigned as intramolecular electron-transfer steps.In the faster of these the tryptophan radical receives an electron from a tyrosine to give a tyrosyl radical product.The tyrosyl radicals formed in both the primary and secondary processes decay within 1 s in contrast to the much longer-lived tyrosyl-122 radical present in active R2 enzyme.Similar results were obtained on pulse radiolysis of the mutant Tyr122Phe R2 protein.Thus the stable Tyr-122 radical form of R2 does not appear to be formed in any of these reactions, and the specificity of the regeneration of the radical in the native enzyme involving reaction of the diiron(II) site with O2 is highlighted.
Ianthesines A-D, four novel dibromotyrosine-derived metabolites from a marine sponge, Ianthella sp.
Okamoto, Yoshihiro,Ojika, Makoto,Kato, Shigemasa,Sakagami, Youji
, p. 5813 - 5818 (2000)
Novel dibromotyrosine-derived metabolites, ianthesines A, B, C, and D, were isolated from an Australian marine sponge of the genus Ianthella sp. Their structures were elucidated using chemical and spectroscopic techniques. Ianthesines A, B, and D were derived from two dibromotyrosines. Ianthesine C is a tetramer possessing eight bromine atoms and its molecular weight is 1606. Ianthesines B-D showed Na,K-ATPase inhibitory activity in the range of 50-440 μM, whereas ianthesine A is inactive. (C) 2000 Elsevier Science Ltd.
Kinetic characterization of O-phospho-L-tyrosine phosphohydrolase activity of two fungal phytases
Ullah, Abul H. J.,Sethumadhavan, Kandan,Mullaney, Edward J.
, p. 7467 - 7471 (2008)
Fungal phytases belonging to "histidine acid phosphatase" or HAP class of phosphohydrolases that catalyze the hydrolysis of phytic acid could also hydrolyze O-phospho-L-tyrosine, which is also called phosphotyrosine. Two phytases from Aspergillus niger and Aspergillus awamori with pH optima 2.5 were tested for phosphotyrosine hydrolase activity; both enzymes cleaved the phosphomonoester bond of phosphotyrosine efficiently at acidic pH. The K m for phosphotyrosine ranged from 465 to 590 μM as opposed to 135 to 160 μM for phytate. The Vmax, however, is 2-4 times higher for phosphotyrosine than it is for phytate. The catalytic efficiency of phytase for phosphotyrosine is on the same order as it is for phytate (3.5 × 10 6 to 1.6 × 107 M-1 s-1); the pH versus activity profile for phosphotyrosine is, however, different from what it is for phytate. The temperature optima shifted 5°C higher to 70°C when phosphotyrosine was used as the substrate. Taken together, the kinetic data show that fungal HAPs that are known as PhyB are capable of cleaving the phosphomonoester bond in phosphotyrosine. This is the first time that phosphotyrosine phosphatase (PTPase) activity has been reported for the subgroup of HAP known as phytase.
Aromatic hydroxylations by flavins: Evidence on direct attack of phenylalamine by flavin radical species
Mager,Tu
, p. 5287 - 5298 (1994)
In 0.05 - 12.0 N acidic solutions, the 5-ethyl-3-methyllumiflavosemiquinone 5 (and/or 5H+) spontaneously arose from the corresponding flavinium cation 4. Raising the temperature from 20 to 50°C, considerably increased the reaction rates with no significant changes in the yields of 5 (5H+). The spontaneous one-electron reduction of 4 requires a coupling with a one-electron oxidation of another flavin such as 5-ethyl-4(a)-hydroxy-3-methyl-4(a),5-dihydroflavin pseudobase 1. The latter, being in equilibrium with 4, can be oxidized to give the transient 5-ethyl-4(a)-hydroxy-3-methyllumiflavin radical 2. This is the protonated form of a flavinoxy radical 3(a,b), a product of a homolysis of the O-O bond in a dihydroflavin hydroperoxide. As an alternative to the homolysis mentioned, the one-electron oxidation of 1 provides the principle to develop a new hydroxylating model system that does not require a dihydroflavin hydroperoxide as a starting compound. Using phenylalanine as a test substrate, the anaerobic formation of tyrosine and its o- and m-hydroxyphenylalanine isomers was established. This achievement is a strong experimental support for the hypothesis that flavin radical species like 2 may directly attack an aromatic. Evidence was obtained on some accumulation of an intermediate that is not a hydroxycyclohexadienyl radical. It was shown to react in a secondary, oxidative chain reaction, remarkably increasing the yields of aromatic hydroxylation without any further supply of flavin.
Reversibility of Charge Transfer between Tryptophan and Tyrosine
Butler, John,Land, Edward J.,Pruetz, Walter A.,Swallow, A. John
, p. 348 - 349 (1986)
Whereas tryptophan radicals oxidise tyrosine over a wide range of pH values, the one-electron reduction potential of the electron-deficient tryptophan radical at pH 7 is only 0.093 V more positive than that of the corresponding tyrosine radical, so that the reaction proceeds in reverse in strongly acid and alkaline solution.
Tyrosine formation from phenylalanine by ultraviolet irradiation
Ishimitsu,Fujimoto,Ohara
, p. 1417 - 1418 (1990)
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Synthesis of L tyrosine or 3,4 dihydroxyphenyl L alanine from DL serine and phenol or pyrocathechol
Enei,Matsui,Nakazawa,et al.
, p. 493 - 499 (1973)
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Characterization of diketopiperazine heterodimers as potential chemical markers for discrimination of two dominant black aspergilli, Aspergillus niger and Aspergillus tubingensis
Deng, Ning,Li, Wei,Ren, Guang-Wei,Wang, Xiao-Qiang,Wang, Xiu-Fang,Xu, Ce,Xu, Kuo,Yuan, Xiao-Long,Zhang, Peng
, (2020)
Black aspergilli are distributed worldwide and represent one of the most prolific sources of metabolites with biomedical and agrochemical interests. However, due to their similar morphological characteristics and insufficient molecular identification, the taxonomic classification of black aspergilli remains ill-defined. The production of specialised metabolites is often unique for species among black aspergilli and could be used as diagnostic chemical markers for species identification. In this study, chemical investigation of Aspergillus tubingensis OUCMBIII 143291 led to the discovery of the diagnostic chemical marker asperazine, a complex diketopiperazine heterodimer, as well as two previously undescribed analogues, asperazine B and C. In addition, an undescribed 2-benzylpyridin-4(1H)-one-containing amide, pestalamide D, along with four known related metabolites were isolated. Their chemical structures, including their absolute configurations, were established on the basis of comprehensive spectral analysis and chiral HPLC analysis of the acidic hydrolysates. Asperazines B and C can serve as potential chemical markers for distinguishing A. tubingensis from A. niger, two representative species of black aspergilli that are usually incorrectly identified. Moreover, the isolated compounds were evaluated for their antifungal activity against eight phytopathogenic fungi including Alternaria alternata, A. brassicae, Botrytis cinerea, Colletotrichum lagenarium, Fusarium oxysporum, Gaeumannomyces graminis, Penicillium digitatum, and Valsa mali. Pestalamide D exhibited significant activities against B. cinerea, C. lagenarium, and V. mali, with MIC values of 4, 8, and 8 μg/mL, respectively, compared with the positive controls carbendazim (MICs = 8, 4, and 4 μg/mL) and prochloraz (MICs = 8, 8, and 4 μg/mL). The results of this study reveal two additional chemical markers and provide a powerful tool for the rapid identification of black aspergilli.
Effects of three peptidase inhibitors, amastatin, captopril and phosphoramidon, on the hydrolysis of [Met5]-enkephalin-Arg6-Phe7 and other opioid peptides
Hiranuma, Toyokazu,Kitamura, Ken,Taniguchi, Takao,Kobayashi, Tomomi,Tamaki, Raita,Kanai, Masayuki,Akahori, Kazuhito,Iwao, Kayoko,Oka, Tetsuo
, p. 276 - 282 (1998)
The contents of [Met5]-enkephalin-Arg6-Phe7 (met-enk-RF) and its six hydrolysis products: Y, YG, YGG, YGGF, YGGFM, and YGGFMR were estimated after incubating met-enk-RF with either a guinea-pig ileal or striatal membrane fraction for various times at 37°C. After 45 min incubation with either ileal or striatal membranes, met-enk-RF was completely hydrolyzed, yielding Y as the major product. Incubation with either membrane preparation for 60 min in the presence of the aminopeptidase inhibitor amastatin hydrolyzed 90 or 92% of met-enk-RF, respectively, with YGG being the major product. If the dipeptidyl carboxypeptidase I inhibitor captopril is also included in the incubation, met-enk-RF hydrolysis decreases by about half for both membranes, with YGG remaining the major product. Inclusion of three peptidase inhibitors, amastatin, captopril, and phosphoramidon (inhibition of endopeptidase-24.11) further reduced met-enkhydrolysis, with 87% or more remaining intact. This shows that met-enk-RF was mainly hydrolyzed by three enzymes, amastatin-sensitive aminopeptidase, captopril-sensitive dipeptidyl carboxypeptidase I and phosphoramidon-sensitive endopeptidase-24.11, in both ileal and striatal membranes. Additionally, estimations of [Leu5]-enkephalin (leu-enk), α- and β-neoendorphins (α- and β-neoends), and dynorphin B (dyn B) contents after incubating the individual peptides with striatal membrane for 60 min in the presence of the three peptidase inhibitors showed that 98, 32, 5, and 23%, respectively, remained intact. Our previous studies together with the data obtained here show that one group of endogenous opioid peptides: met-enk, leu-enk, met-enk-RF, met-enk-RGL, and dyn A-(1-8) are largely or almost exclusively hydrolyzed by the three enzymes, amastatin-sensitive aminopeptidase, captopril-sensitive dipeptidyl carboxypeptidase I, and phosphoramidon-sensitive endopeptidase-24.11, and indicate that an unidentified fourth enzyme(s) is involved in the hydrolysis of another group of peptides: α-neoend, β-neoend, and dyn B.
OXIDATION OF L-PHENYLALANINE BY THE MODIFIED UDENFRIEND SYSTEM
Blanchard, M.,Bouchoule, C.,Djaneye-Boundjou, G.,Canesson, P.
, p. 2177 - 2178 (1988)
L-phenylalanine is oxidized by oxygen into 3,4-dihydroxyphenylalanine (DOPA) at 40 deg C with Fe(2+) EDTA as a catalyst.For the reduction of Fe(3+) species, electrons are released from the cathode of an electrochemical cell.
Minor constituents from the tubers of Gymnadenia conopsea
Zi, Jia-Chen,Lin, Sheng,Zhu, Cheng-Gen,Yang, Yong-Chun,Shi, Jian-Gong
, p. 477 - 484 (2010)
Four new minor constituents including two cyclodipeptides (1 and 2) and two cyclopentene derivatives (3 and 4), together with four known cyclodipeptides, have been isolated from an ethanolic extract of the tubers of Gymnadenia conopsea. Their structures i
An antifungal tetrapeptide from the culture of Penicillium canescens
Bertinetti, Brenda V.,Pena, Nora I.,Cabrera, Gabriela M.
, p. 1178 - 1184 (2009)
A new tetrapeptide D-Phe-L-Val-D-Val-L-Tyr (1), along with three known diketopiperazines and pseurotin A, were isolated from the culture of Penicillium canescens, collected from pollen from beehives, in a screening for new antimicrobial products from unex
Formation of a hydroxyl radical from riboflavin sodium phosphate by photo-illumination
Ishimitsu, Susumu,Mishima, Ikuko,Tsuji, Sumiko,Shibata, Tadashi
, p. 2107 - 2109 (1997)
Photo-illumination of riboflavin sodium phosphate (Rp) with phenylalanine produced significant levels of o-tyrosine, m-tyrosine and p- tyrosine as hydroxylated products. The hydroxylation of Rp was pH-dependent, and the maximum rate was around pH 4.5. Replacement of air with nitrogen prevented the formation of tyrosine isomers while the addition of superoxide dismutase or catalase to this system prevented hydroxylation. The tyrosine formation by the system was significantly prevented by hydroxyl radical (HO·) scavengers such as potassium iodide, potassium bromide, thiourea and sodium formate. No free iron and cupric ions were detected in the reaction mixture by inductively-coupled plasma atomic emission spectrometry. The above results suggest that the formation of HO· may occur in the photochemical reaction system in the presence of Rp under aerobic conditions, and that a superoxide radical and hydrogen peroxide may be involved in HO· formation.
Hydroxylation of phenylalanine by the hypoxanthine-xanthine oxidase system.
Ishimitsu,Fujimoto,Ohara
, p. 4645 - 4649 (1984)
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Enzyme immobilization on smart polymers: Catalysis on demand
Cirillo, Giuseppe,Nicoletta, Fiore Pasquale,Curcio, Manuela,Spizzirri, Umile Gianfranco,Picci, Nevio,Iemma, Francesca
, p. 62 - 69 (2014)
A new approach for the synthesis of hydrogel films with thermo-sensitive enzymatic activity is reported. Pepsin (PEP) was covalently immobilized on thermo-responsive hydrogels by radical polymerization in the presence of N-isopropylacrylamide and poly-(ethylene glycol) dimethacrylate 750, acting as functional monomer and crosslinking agent, respectively. Hydrogels showing lower critical solution temperatures between 32.9 and 36.1 °C were synthesized by UV-irradiation of reaction batches differing in the PEP/monomers ratio. The derivatization degree of the hydrogels was expressed as mg of PEP per gram of matrix and found to be in the range of 6 to 11% as assessed by Lowry method. Scanning electron microscopy analysis and water affinity evaluation allowed to highlight the porous morphology and thermo-responsivity of hydrogels as a function of temperature. Using bovine serum albumin as a substrate, kinetics parameters were determined by Lineweaver-Burk plots and the catalyst efficiency evaluated. The influence of temperature on enzyme activity, as well as the thermal stability and reusability of devices, were also investigated.
Squamins C–F, four cyclopeptides from the seeds of Annona globiflora
Sosa-Rueda, Javier,Domínguez-Meléndez, Vanihamin,Ortiz-Celiseo, Araceli,López-Fentanes, Fernando C.,Cuadrado, Cristina,Fernández, José J.,Daranas, Antonio Hernández,Cen-Pacheco, Francisco
, (2021/08/04)
Four cyclic octapeptides, squamins C–F, were isolated from the seeds of Annona globiflora Schltdl. These compounds share part of their amino acid sequence, -Pro-Met(O)-Tyr-Gly-Thr-, with previously reported squamins A and B. Their structures were determined using NMR spectroscopic techniques together with quantum mechanical calculations (QM-NMR), ESI-HRMS data and a modified version of Marfey's chromatographic method. All compounds showed cytotoxic activity against DU-145 (human prostate cancer) and HeLa (human cervical carcinoma) cell lines. Clearly, A. globiflora is an important source of bioactive molecules, which could promote the sustainable exploitation of this undervalued specie.
Highly Stable Zr(IV)-Based Metal-Organic Frameworks for Chiral Separation in Reversed-Phase Liquid Chromatography
Jiang, Hong,Yang, Kuiwei,Zhao, Xiangxiang,Zhang, Wenqiang,Liu, Yan,Jiang, Jianwen,Cui, Yong
supporting information, p. 390 - 398 (2021/01/13)
Separation of racemic mixtures is of great importance and interest in chemistry and pharmacology. Porous materials including metal-organic frameworks (MOFs) have been widely explored as chiral stationary phases (CSPs) in chiral resolution. However, it remains a challenge to develop new CSPs for reversed-phase high-performance liquid chromatography (RP-HPLC), which is the most popular chromatographic mode and accounts for over 90% of all separations. Here we demonstrated for the first time that highly stable Zr-based MOFs can be efficient CSPs for RP-HPLC. By elaborately designing and synthesizing three tetracarboxylate ligands of enantiopure 1,1′-biphenyl-20-crown-6, we prepared three chiral porous Zr(IV)-MOFs with the framework formula [Zr6O4(OH)8(H2O)4(L)2]. They share the same flu topological structure but channels of different sizes and display excellent tolerance to water, acid, and base. Chiral crown ether moieties are periodically aligned within the framework channels, allowing for stereoselective recognition of guest molecules via supramolecular interactions. Under acidic aqueous eluent conditions, the Zr-MOF-packed HPLC columns provide high resolution, selectivity, and durability for the separation of a variety of model racemates, including unprotected and protected amino acids and N-containing drugs, which are comparable to or even superior to several commercial chiral columns for HPLC separation. DFT calculations suggest that the Zr-MOF provides a confined microenvironment for chiral crown ethers that dictates the separation selectivity.
Method for photolysis of amido bonds
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Paragraph 0046; 0048-0049; 0098-0101, (2021/06/26)
The invention discloses a method for photo-splitting amido bonds, wherein the method is mild in reaction condition and can realize splitting of amido bonds by using illumination. The method for photo-splitting the amido bonds comprises the following steps: reacting 2,4-dinitrofluorobenzene with an amino group of a substance which contains alpha amino acid at the tail end and is shown as a structural formula I to generate a compound 1 represented by a structural formula II; and under light irradiation, carrying out amido bond cleavage reaction on the compound 1, wherein R1 is a side chain group of alpha-amino acid, and R2 is aryl, aliphatic hydrocarbon, -CH(R)-COOH or polypeptide.
