Netropsin
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| Category | Antineoplastic |
| Catalog number | BBF-02601 |
| CAS | 1438-30-8 |
| Molecular Weight | 430.47 |
| Molecular Formula | C18H26N10O3 |
| Purity | ≥98% |
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Description
Netropsin is isolated from Streptomyces netropsis as a basic polypeptide. It can specific bind to A-T areas of DNA that is very useful to genetic research. Netropsin can disrupt the cell cycle, prolonging G and arresting in G. Netropsin has antibiotic and antiviral activity. It has been shown that Netropsin is active against Gram-positive and Gram-negative bacteria.
Specification
| Related CAS | 63770-20-7 (hydrochloride) |
| Synonyms | Antibiotic 1142; Antibiotic T-1384; Antibiotic T 1384; Sinanomycin; Congocidin; Congocidine; F6; F-9; IA-887; IA 887; K-117; K 117; N-(3-amino-3-iminopropyl)-4-(4-(2-guanidinoacetamido)-1-methyl-1H-pyrrole-2-carboxamido)-1-methyl-1H-pyrrole-2-carboxamide |
| Shelf Life | 2 years |
| Storage | Store at -20°C |
| IUPAC Name | N-[5-[(3-amino-3-iminopropyl)carbamoyl]-1-methylpyrrol-3-yl]-4-[[2-(diaminomethylideneamino)acetyl]amino]-1-methylpyrrole-2-carboxamide |
| Canonical SMILES | CN1C=C(C=C1C(=O)NC2=CN(C(=C2)C(=O)NCCC(=N)N)C)NC(=O)CN=C(N)N |
| InChI | InChI=1S/C18H26N10O3/c1-27-9-11(6-12(27)16(30)23-4-3-14(19)20)26-17(31)13-5-10(8-28(13)2)25-15(29)7-24-18(21)22/h5-6,8-9H,3-4,7H2,1-2H3,(H3,19,20)(H,23,30)(H,25,29)(H,26,31)(H4,21,22,24) |
| InChI Key | IDBIFFKSXLYUOT-UHFFFAOYSA-N |
Properties
| Appearance | Solid Powder |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Gram-negative bacteria; mycobacteria; fungi; neoplastics (Tumor); viruses |
| Boiling Point | 760.5°C at 760 mmHg |
| Melting Point | 171-173°C |
| Density | 1.3374 g/cm3 |
Reference Reading
1. Mechanism for the Binding of Netropsin to Hairpin DNA Revealed Using Nanoscale Ion Emitters in Native Mass Spectrometry
William A Donald, Giang T H Nguyen, Vincent Murray, Huixin Wang, Wai Yu Leung, Thinh N Tran Anal Chem . 2020 Jan 7;92(1):1130-1137. doi: 10.1021/acs.analchem.9b04209.
Netropsin is one of the first ligands to be discovered that selectively binds to the minor groove of DNA and is actively used as a scaffold for developing potential anticancer and antibiotic agents. The mechanism by which netropsin binds to hairpin DNA remains controversial with two competing mechanisms having been proposed. In one mechanism, netropsin binding induces a hairpin-to-duplex DNA transition. Alternatively, netropsin binds in two thermodynamically different modes at a single duplexed AATT site. Here, results from native mass spectrometry (MS) with nanoscale ion emitters indicate that netropsin can simultaneously and sequentially bind to both hairpin and duplex DNA. Duplex DNA was not detected using conventional MS with larger emitters because nanoscale emitters significantly reduce the extent of salt adduction to ligand-DNA complex ions, including in the presence of relatively high concentrations of nonvolatile salts. Based on native MS and polyacrylamide gel electrophoresis results, the abundances of hairpin and duplex DNA are unaffected by the addition of netropsin. By native MS, the binding affinities for five ligand-DNA and DNA-DNA interactions can be rapidly obtained simultaneously. This research indicates a "simultaneous binding mechanism" for the interactions of netropsin with DNA.
2. Netropsin and bis-netropsin analogs as inhibitors of the catalytic activity of mammalian DNA topoisomerase II and topoisomerase cleavable complexes
K E Rao, L S Gawron, T A Beerman, J M Woynarowski, R D Sigmund, J W Lown Biochim Biophys Acta . 1991 Aug 27;1090(1):52-60. doi: 10.1016/0167-4781(91)90036-l.
This study examined the ability of netropsin and related minor groove binders to interfere with the actions of DNA topoisomerases II and I. We evaluated a series of netropsin dimers linked with flexible aliphatic chains of different lengths. These agents are potentially able to occupy longer stretches of DNA than the parental drug as a result of bidentate binding. Both netropsin and its dimers were found: (i) to inhibit the catalytic activity of isolated topoisomerase II and (ii) to interfere with the stabilization of the cleavable complexes of topoisomerase II and I in nuclei. Dimers with linkers consisting of 0-4 and 6-9 methylene groups (n) were far more inhibitory than netropsin against isolated enzyme and in the nuclear system. The compound with n = 5 was less active than netropsin in both assays while the dimer with n = 10 inhibited only the isolated enzyme. The comparison of dimers with fixed linker length (n = 2) but varying number of N-methylpyrrole residues (from 1 to 3) revealed that the inhibitory properties were enhanced with increasing number of N-methylpyrrole units. For dimers with varying linker length, drug ability to inhibit catalytic activity of isolated topoisomerase II was positively correlated with calf thymus DNA association constants. In contrast, no such correlation existed in nuclei. However, the inhibitory effects in the nuclear system were correlated with the association constants for poly(dAdT). The results indicate that bidentate binding can significantly enhance anti-topoisomerase activity of netropsin related dimeric minor groove binders. However, other factors such as the length of the linker, the number of pyrrole moieties and the nature of the target (isolated enzyme/DNA versus chromatin in nuclei) also contribute to these activities.
3. Netropsin, a minor groove binding ligand: a potential radioprotective agent
R Bhardwaj, K Mishra, N K Chaudhury Radiat Res . 2009 Dec;172(6):698-705. doi: 10.1667/RR1815.1.
Minimizing radiation-induced damages in DNA is an important aspect in the development of chemical radioprotectors. The aim of this study was to evaluate the possible radioprotective ability of the DNA minor groove binding ligand netropsin in an aqueous solution of plasmid DNA (pBR322) and to compare its efficacy with that of Hoechst 33258, a known radioprotector. The radiochemical parameters D(0), G(SSB) and DMF were calculated in pBR322 DNA. Based on a comparison of the DMFs of netropsin and Hoechst 33258, netropsin appeared to be the better radioprotector. The ligand binding site accessibility of the restriction enzyme EcoRI at the ligand-pBR322 complex was assessed using a restriction-digestion assay in irradiated solutions. A distinct ligand-bound site protection in netropsin-DNA was observed in irradiated solutions. However, no site protection was observed in the presence of Hoechst 33258. The possible role of ligand-induced structural stabilization in irradiated aqueous solutions was also investigated using netropsin-calf thymus DNA melting temperature measurements. The greater radioprotective ability of netropsin in solutions of DNA was suggested to be due to its higher binding affinity and its ability to provide higher structural stabilization. EcoRI digestion revealed that hydroxyl radical (OH*) generated by ionizing radiation is not able to radiolyse the netropsin-DNA complex. These results will help in developing better radioprotectors.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
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Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
