cas 21820-51-9, O-PHOSPHO-L-TYROSINE | Articles data

Articles about 21820-51-9Total 10 be found

Enzymatically Forming Intranuclear Peptide Assemblies for Selectively Killing Human Induced Pluripotent Stem Cells
Tumorigenic risk of undifferentiated human induced pluripotent stem cells (iPSCs), being a major obstacle for clinical application of iPSCs, requires novel approaches for selectively eliminating undifferentiated iPSCs. Here, we show that an l-phosphopenta
He, Hongjian,Liu, Shuang,Lu, Shijiang,Shy, Adrianna N.,Xu, Bing,Yi, Meihui,Zhang, Qiuxin
supporting information
p. 15852 - 15862
(2021/10/02)

Asymmetric catalytic synthesis method of L-tyrosine derivative
The invention relates to an asymmetric catalytic synthesis method of an L-tyrosine derivative, which comprises the following steps of: reacting a compound as shown in a formula (II) with a compound as shown in a formula (III) in the presence of a catalyst as shown in a formula (A), and hydrolyzing to obtain a compound as shown in a formula (I). When the method is used for preparing derivatives such as phosphoric acid or phosphate of L-tyrosine, a large amount of strong acid such as phosphoric acid does not need to be used, the equipment requirement is lowered, the production safety is improved, a large amount of alkali does not need to be adopted for neutralization in post-treatment, generation of a large amount of waste residues such as inorganic salt is avoided, and high economic and environment protection effects are achieved.
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Paragraph 0098-0100

(2021/09/08)

Enzyme Instructed Self-assembly of Naphthalimide-dipeptide: Spontaneous Transformation from Nanosphere to Nanotubular Structures that Induces Hydrogelation
Understanding the structure-morphology relationships of self-assembled nanostructures is crucial for developing materials with the desired chemical and biological functions. Here, phosphate-based naphthalimide (NI) derivatives have been developed for the
Chakravarthy, Rajan Deepan,Lin, Hsin-Chieh,Mohammed, Mohiuddin
supporting information

(2020/08/03)

Modified synthesis method of oxidative phosphorylation-L-tyrosine
The invention discloses a modified synthesis method of oxidative phosphorylation-L-tyrosine, and belongs to the field of organic chemistry. L-tyrosine and phosphorus pentoxide are reacted in 85% strong phosphoric acid, a molar ratio of the L-tyrosine to t
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Paragraph 0022-0023; 0025-0026; 0028-0029; 0030-0032

(2019/01/14)

An in situ Dynamic Continuum of Supramolecular Phosphoglycopeptides Enables Formation of 3D Cell Spheroids
Higher-order assemblies of proteins, with a structural and dynamic continuum, is an important concept in biology, but these insights have yet to be applied in designing biomaterials. Dynamic assemblies of supramolecular phosphoglycopeptides (sPGPs) transf
Wang, Huaimin,Shi, Junfeng,Feng, Zhaoqianqi,Zhou, Rong,Wang, Shiyu,Rodal, Avital A.,Xu, Bing
supporting information
p. 16297 - 16301
(2017/11/27)

Enzyme-instructed self-assembly with photo-responses for the photo-regulation of cancer cells
Using a short peptide precursor modified by the biaryltetrazole with intramolecular photo-click reactivity, we realized the photo-regulation of the pericellular nanofibers formed by the enzyme-instructed self-assembly on the cell membrane. Upon light irra
Zhou, Zhengquan,Xie, Xian,Yi, Qikun,Yin, Wencui,Kadi, Adnan A.,Li, Jinbo,Zhang, Yan
supporting information
p. 6892 - 6895
(2017/09/01)

Synthesis of six phenylalanine derivatives and their cell toxicity effect on human colon cancer cell line HT-29
Some phenylalanine (Phe) derivatives had important roles in pharmacology and may be used as pharmaceutical materials and pharmaceutical intermediates. In order to understand the cell toxicity of phenylalanine derivatives, we synthesized L-4-bromo-phenylalanine (Brp), L-4-iodophenylalanine (Ip), L-4-nitro-phenylalanine (Np), L-4-sulfonic-phenylalanine (Sp), L-4-phosphophenylalanine (Pp) and L-4-amino-phenylalanine (Np). We used mass spectrometry (MS), Infrared Spectroscopy (IR) or hydrogen-1 nuclear magnetic resonance spectrum (1H-NMR), and high performance liquid chromatography (HPLC) to test the correction of these products, MTT assay and Hoechst 33258 staining to detect their cell toxic effect on human colon cancer cell HT-29 (HT-29 cells). The results showed that these products were correct and the cytotoxicity of Pp>Ip>Sp and Np>Brp, Ap almost had no effect on HT-29 cells. In addition, Pp, Ip and Sp induced cell apoptosis, the other three kinds of phenylalanine derivatives induced neither apoptosis nor necrosis.
Zhao, Qianyi,Xu, Ting,Li, Menghua,Yang, Ying,Hu, Haopeng,Wang, Shupei,Yan, Wenjuan,Chen, Ran,Zhang, Chunyan,Xu, Cunshuan
p. 466 - 470
(2015/06/22)

Thiophosphorylation of free amino acids and enzyme protein by thiophosphoramidate ions
In search of an activity-preserving protein thiophosphorylation method, with thymidylate synthase recombinant protein used as a substrate, potassium thiophosphoramidate and diammonium thiophosphoramidate salts in Tris- and ammonium carbonate based buffer solutions were employed, proving to serve as a non-destructive environment. Using potassium phosphoramidate or diammonium thiophosphoramidate, a series of phosphorylated and thiophosphorylated amino acid derivatives was prepared, helping, together with computational (using density functional theory, DFT) estimation of 31P NMR chemical shifts, to assign thiophosphorylated protein NMR resonances and prove the presence of thiophosphorylated lysine, serine and histidine moieties. Methods useful for prediction of 31P NMR chemical shifts of thiophosphorylated amino acid moieties, and thiophosphates in general, are also presented. The preliminary results obtained from trypsin digestion of enzyme shows peak at m/z 1825.805 which is in perfect agreement with the simulated isotopic pattern distributions for monothiophosphate of TVQQQVHLNQDEYK where thiophosphate moiety is attached to histidine (His26) or lysine (Lys33) side-chain.
Ruman, Tomasz,Dlugopolska, Karolina,Jurkiewicz, Agata,Rut, Dagmara,Fraczyk, Tomasz,Ciesla, Joanna,Les, Andrzej,Szewczuk, Zbigniew,Rode, Wojciech
experimental part
p. 74 - 80
(2010/05/17)

Phosphorylation of enkephalins enhances their proteolytic stability
Pharmacological action of enkephalins as opioid peptides is limited because of their rapid degradation by endoproteases. A novel approach is used in this study to prolong the life of those peptides. Phosphorylation of N-terminal tyrosine residue is found to have a profound influence in improving the stability of [Met]enkephalin and [Leu]enkephalin against the action of aminopeptidase M. Whereas, breakdown of [Met]enkephalin and [Leu]enkephalin is essentially complete in less than one min when incubated at 37°C with purified aminopeptidase M (EC 3.4.11.2; substrate:enzyme = 1:0.1) in Tris buffer (pH 7.02), the corresponding phospho analogs are still detected 60 min after start of incubation. The rate of disappearance of phospho-[Met]enkephalin and phospho-[Leu]enkephalin follows first-order kinetics with half-lives of 7.3 and 8.8 min, respectively.
Dass, Chhabil,Mahalakshmi
p. 1039 - 1045
(2007/10/03)