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methyl 8–oxo–8-((trityloxy)amino)octanoate is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

449729-22-0

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449729-22-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 449729-22-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 4,4,9,7,2 and 9 respectively; the second part has 2 digits, 2 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 449729-22:
(8*4)+(7*4)+(6*9)+(5*7)+(4*2)+(3*9)+(2*2)+(1*2)=190
190 % 10 = 0
So 449729-22-0 is a valid CAS Registry Number.

449729-22-0Relevant academic research and scientific papers

Design and synthesis of parthenolide-SAHA hybrids for intervention of drug-resistant acute myeloid leukemia

Ge, Weizhi,Liu, Zhongquan,Sun, Yu,Wang, Tianpeng,Guo, Hongyu,Chen, Xinyi,Li, Shengzu,Wang, Mengmeng,Chen, Yue,Ding, Yahui,Zhang, Quan

, p. 699 - 713 (2019)

A series of parthenolide-SAHA hybrids were synthesized and evaluated for their anti-AML activities against HL-60 and HL-60/ADR cell lines. The most active compound 26 exhibited high activity against HL-60/ADR cell line with IC50 value of 0.15 μ

Structurally Diverse Histone Deacetylase Photoreactive Probes: Design, Synthesis, and Photolabeling Studies in Live Cells and Tissue

Aboukhatwa, Shaimaa M.,Hanigan, Thomas W.,Taha, Taha Y.,Neerasa, Jayaprakash,Ranjan, Rajeev,El-Bastawissy, Eman E.,Elkersh, Mohamed A.,El-Moselhy, Tarek F.,Frasor, Jonna,Mahmud, Nadim,McLachlan, Alan,Petukhov, Pavel A.

supporting information, p. 1096 - 1107 (2019/04/17)

Histone deacetylase (HDAC) activity is modulated in vivo by post-translational modifications and formation of multiprotein complexes. Novel chemical tools to study how these factors affect engagement of HDAC isoforms by HDAC inhibitors (HDACi) in cells and tissues are needed. In this study, a synthetic strategy to access chemically diverse photoreactive probes (PRPs) was developed and used to prepare seven novel HDAC PRPs 9–15. The class I HDAC isoform engagement by PRPs was determined in biochemical assays and photolabeling experiments in live SET-2, HepG2, HuH7, and HEK293T cell lines and in mouse liver tissue. Unlike the HDAC protein abundance and biochemical activity against recombinant HDACs, the chemotype of the PRPs and the type of cells were key in defining the engagement of HDAC isoforms in live cells. Our findings suggest that engagement of HDAC isoforms by HDACi in vivo may be substantially modulated in a cell- and tissue-type-dependent manner.

Phenylalanine-containing hydroxamic acids as selective inhibitors of class IIb histone deacetylases (HDACs)

Schaefer, Stefan,Saunders, Laura,Eliseeva, Elena,Velena, Alfredo,Jung, Mira,Schwienhorst, Andreas,Strasser, Anja,Dickmanns, Achim,Ficner, Ralf,Schlimme, Sonja,Sippl, Wolfgang,Verdin, Eric,Jung, Manfred

, p. 2011 - 2033 (2008/09/21)

We synthesized biarylalanine-containing hydroxamic acids and tested them on immunoprecipitated HDAC1 and HDAC6 and show a subtype selectivity for HDAC6 that was confirmed in cells by Western blot (tubulin vs histones). We obtained an X-ray structure with

Structure-activity relationships on phenylalanine-containing inhibitors of histone deacetylase: In vitro enzyme inhibition, induction of differentiation, and inhibition of proliferation in friend leukemic cells

Wittich, Sybille,Scherf, Hans,Xie, Changping,Brosch, Gerald,Loidl, Peter,Gerh?user, Clarissa,Jung, Manfred

, p. 3296 - 3309 (2007/10/03)

Inhibitors of histone deacetylases (HDACs) are a new class of anticancer agents that affect gene regulation. We had previously reported the first simple synthetic HDAC inhibitors with in vitro activity at submicromolar concentrations. Here, we present structure-activity data on modifications of a phenylalanine-containing lead compound including amino acid amides as well as variations of the amino acid part. The compounds were tested for inhibition of maize HD-2, rat liver HDAC, and for the induction of terminal cell differentiation and inhibition of proliferation in Friend leukemic cells. In the amide series, in vitro inhibition was potentiated up to 15-fold, but the potential to induce cell differentiation decreased. Interestingly, an HDAC class selectivity was indicated among some of these amides. In the amino acid methyl ester series, a biphenylalanine derivative was identified as a good enzyme inhibitor, which blocks proliferation in the submicromolar range and is also a potent inducer of terminal cell differentiation.

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