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(Synonyms: 嘌呤霉素二盐酸盐水合物) 目录号 : GC32186

Puromycin 2HCl (CL13900) is an aminonucleoside antibiotic, which acts as a protein synthesis inhibitor.

Puromycin (CL13900) Chemical Structure

Cas No.:53-79-2

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产品描述

Puromycin 2HCl (CL13900) is an aminonucleoside antibiotic, which acts as a protein synthesis inhibitor.

The antibiotic puromycin is produced by the actinoniycete, Streptornyces alboniger, and has been used as a tool for studying protein synthesis in a number of systems. [1] Puromycin can be used for the selection of recombinant cells from noncultured cells. [2]

Puromycin (aminonucleoside) inhibits protein synthesis leading to proteinuria & glomerulosclerosis/nephrosis.[4]

2HCl盐酸盐嘌呤霉素(Puromycin 2HCl,CL13900)是一种氨基核苷类抗生素,可作为蛋白质合成抑制剂。

嘌呤霉素抗生素由放线菌白色素链霉菌(Streptornyces alboniger)产生,并已用于许多系统中研究蛋白质合成。[1] 嘌呤霉素可用于从非培养细胞中选择重组细胞。[2]

嘌呤霉素(氨基核苷类)抑制蛋白质合成,导致蛋白尿和肾小球硬化/肾病综合征。[4]

[1] Darken MA. Pharmacol Rev. 1964, 16, 223-243. [2] Watanabe S, et al. Biol Reprod. 2005, 72(2), 309-315. [3] Chan C, et al. Pharmacol Res Perspect. 2017 Oct;5(5):e00359.

Chemical Properties

Cas No. 53-79-2 SDF
别名 嘌呤霉素二盐酸盐水合物
Canonical SMILES OC[C@@H]1[C@@H](NC([C@@H](N)CC2=CC=C(OC)C=C2)=O)[C@H]([C@H](N3C=NC4=C3N=CN=C4N(C)C)O1)O
分子式 C22H29N7O5 分子量 471.51
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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1 mM 2.1208 mL 10.6042 mL 21.2085 mL
5 mM 0.4242 mL 2.1208 mL 4.2417 mL
10 mM 0.2121 mL 1.0604 mL 2.1208 mL
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Research Update

Optical Control of Translation with a Puromycin Photoswitch

J Am Chem Soc 2022 Nov 30;144(47):21494-21501.PMID:36394560DOI:10.1021/jacs.2c07374.

Translation is an elementary cellular process that involves a large number of factors interacting in a concerted fashion with the ribosome. Numerous natural products have emerged that interfere with the ribosomal function, such as Puromycin, which mimics an aminoacyl tRNA and causes premature chain termination. Here, we introduce a photoswitchable version of Puromycin that, in effect, puts translation under optical control. Our compound, termed puroswitch, features a diazocine that allows for reversible and nearly quantitative isomerization and pharmacological modulation. Its synthesis involves a new photoswitchable amino acid building block. Puroswitch shows little activity in the dark and becomes substantially more active and cytotoxic, in a graded fashion, upon irradiation with various wavelengths of visible light. In vitro translation assays confirm that puroswitch inhibits translation with a mechanism similar to that of Puromycin itself. Once incorporated into nascent proteins, puroswitch reacts with standard Puromycin antibodies, which allows for tracking de novo protein synthesis using western blots and immunohistochemistry. As a cell-permeable small molecule, puroswitch can be used for nascent proteome profiling in a variety of cell types, including primary mouse neurons. We envision puroswitch as a useful biochemical tool for the optical control of translation and for monitoring newly synthesized proteins in defined locations and at precise time points.

Puromycin Prodrug Activation by Thioredoxin Reductase Overcomes Its Promiscuous Cytotoxicity

J Med Chem 2023 Mar 9;66(5):3250-3261.PMID:36855911DOI:10.1021/acs.jmedchem.2c01509.

Overexpression of the selenoprotein thioredoxin reductase (TrxR) has been documented in malignant tissues and is of pathological significance for many types of tumors. The antibiotic Puromycin (Puro) is a protein synthesis inhibitor causing premature polypeptide chain termination during translation. The well-defined action mechanism of Puro makes it a useful tool in biomedical studies. However, the nonselective cytotoxicity of Puro limits its therapeutic applications. We report herein the construction and evaluation of two Puro prodrugs, that is, S1-Puro with a five-membered cyclic disulfide trigger and S2-Puro with a linear disulfide trigger. S1-Puro is selectively activated by TrxR and shows the TrxR-dependent cytotoxicity to cancer cells, while S2-Puro is readily activated by thiols. Furthermore, S1-Puro displays higher stability in plasma than S2-Puro. We expect that this prodrug strategy may promote the further development of Puro as a therapeutic agent.

Puromycin reactivity does not accurately localize translation at the subcellular level

Elife 2020 Aug 26;9:e60303.PMID:32844748DOI:10.7554/eLife.60303.

Puromycin is a tyrosyl-tRNA mimic that blocks translation by labeling and releasing elongating polypeptide chains from translating ribosomes. Puromycin has been used in molecular biology research for decades as a translation inhibitor. The development of Puromycin antibodies and derivatized Puromycin analogs has enabled the quantification of active translation in bulk and single-cell assays. More recently, in vivo puromycylation assays have become popular tools for localizing translating ribosomes in cells. These assays often use elongation inhibitors to purportedly inhibit the release of puromycin-labeled nascent peptides from ribosomes. Using in vitro and in vivo experiments in various eukaryotic systems, we demonstrate that, even in the presence of elongation inhibitors, puromycylated peptides are released and diffuse away from ribosomes. Puromycylation assays reveal subcellular sites, such as nuclei, where puromycylated peptides accumulate post-release and which do not necessarily coincide with sites of active translation. Our findings urge caution when interpreting puromycylation assays in vivo.

Puromycin based inhibitors of aminopeptidases for the potential treatment of hematologic malignancies

Eur J Med Chem 2017 Oct 20;139:325-336.PMID:28803047DOI:10.1016/j.ejmech.2017.07.048.

Substantial progress has been described in the study of Puromycin and its analogs for antibiotic properties. However, the peptidase inhibitory activity of related analogs has not been explored as extensively. Specifically, inhibiting aminopeptidases for achieving antitumor effect has been sparsely investigated. Herein, we address this challenge by reporting the synthesis of a series of analogs based on the structural template of Puromycin. We also present exhaustive biochemical and in vitro analyses in support of our thesis. Analyzing the structure-activity relationship revealed a steric requirement for maximum potency. Effective inhibitors of Puromycin-Sensitive Aminopeptidase (PSA) are disclosed here. These potential therapeutic agents display superior in vitro antitumor potency against two leukemic cell lines, as compared to known inhibitors of aminopeptidases.

A New Photocaged Puromycin for an Efficient Labeling of Newly Translated Proteins in Living Neurons

Chembiochem 2018 Dec 4;19(23):2458-2464.PMID:30311996DOI:10.1002/cbic.201800408.

Monitoring newly synthesized proteins is becoming increasingly important to characterize proteome composition in regulatory networks. Puromycin is a peptidyl transfer inhibitor, widely used in cell biology for tagging newly synthesized proteins. Here, we report synthesis and application of an optimized Puromycin carrying a photolabile protecting group as a powerful tool for tagging nascent proteins with high spatiotemporal resolution. The photocaged 7-N,N-(diethylaminocumarin-4-yl)-methoxycarbonyl-puromycin (DEACM-puromycin) was synthesized and compared with the previously developed 6-nitroveratryloxycarbonyl Puromycin (NVOC-puromycin). The photochemical behavior as well as the effectiveness in controlling puromycylation in living hippocampal neurons using two-photon excitation is superior to the previously used NVOCpuromycin. We further report on the application of light-controlled puromycylation to visualize new translated proteins in neurons.