Correction: McLoughlin, E.C.; O’Boyle, N.M. Colchicine-Binding Site Inhibitors from Chemistry to Clinic: A Review. Pharmaceuticals 2020, 13, 8

McLoughlin, Eavan; O’Boyle, Niamh M.

doi:10.3390/ph13040072

Cited by 51 publications

(21 citation statements)

References 2 publications

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“…However, understanding of the mechanism of NLRP3 activation, as well as the role of activators and inhibitors of this process is still unclear, expecially at molecular level. Colchicine -a compound that has been shown to be effective in diseases associated with NLRP3 such as gout, cardiovascular disease [7] has been shown experimentally to affect the NLRP3 pathway, inhibit protein expression of cleaved caspase-1 and mature IL-1, such as suppressing IL-1β production. COL can inhibit the expression of the pyrin (MEFV) gene, preventing the assembly of NLRP3 inflammasome, has potent inhibition of P2X7-induced pore formation and the result is blocking the activity of the NLRP3 inflammasome [8].…”

Section: Introductionmentioning

confidence: 99%

Evaluation of Colchicine’s interaction with the ATP-binding region of mice NLRP3-NACHT domain using molecular docking and dynamics simulation

Lai

Nguyen

2022

J. Phys.: Conf. Ser.

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Since the discovery of the role of NLRP3 in microbial infection in 2001, many studies have shown that NLRP3 play a key role in causing many mammal acute and chronic diseases. However, a full understanding of the mechanism of NLRP3 activation is still lacking. Our previous theoretical work and experimental evidence show the role of ATP in interacting with and activating the NATCH region of NLRP3. In this study, we continue to use bioinformatics and molecular dynamic (MD) simulation to evaluate the competitive impact of the interaction the ligand ATP and colchicine (COL) with this NACHT protein. The later ligand is a medication to treat gout attacks. Our results show that COL bind stably to the ATP binding pocket of mice NACHT domain with high numbers of hydrophobic and van der Waals interactions, while hydrogen bond and electrostatic interactions are important types of contact for keeping ATP at its NACHT pocket. Our results assist in building in-silico screening model for natural compounds with pharmacological effects to NLRP3 similar to colchicine with few side effects. In addition, this work helps to better understand the balance between this inflammasome activation and inhibition, which will help in the improvement and development of new therapies for related diseases.

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Section: Introductionmentioning

confidence: 99%

Evaluation of Colchicine’s interaction with the ATP-binding region of mice NLRP3-NACHT domain using molecular docking and dynamics simulation

Lai

Nguyen

2022

J. Phys.: Conf. Ser.

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“…2 Most of these molecules act by binding to the protein tubulin. [3][4][5][6][7][8] There are several binding sites on the tubulin heterodimer, including for vinca alkaloids, taxanes, colchicine, and laulimalide, 8 which are usually divided into two categories: microtubule stabilizers, including taxanes and laulimalide, which enhance tubulin polymerization; and microtubule depolymerizers, including vinca alkaloids and colchicine binding site agents, which inhibit tubulin polymerization. The microtubule destabilizers currently in clinical use include vinca alkaloids, vinblastine, vincristine, and vinorelbine, all of which bind to what has been termed the "vinca site" on tubulin.…”

Section: Introductionmentioning

confidence: 99%

Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design

Lei

Jinghong

et al. 2021

RSC Adv.

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“…On the contrary, stabilizing agents such as taxanes (paclitaxel (IV) or docetaxel (V)) enhance tubulin polymerization and microtubules stabilization (Figure 1). [14][15] Despite the interesting efficacy of MTAs in cancer treatment, serious adverse side effects associated with their long-and short-term use, affect their clinical application. Particularly, neurological and hematological problems represent the widely limiting side effects and also several other toxicities could occur during the use of these drugs.…”

Section: Introductionmentioning

confidence: 99%

α–ω Alkenyl‐bis‐S‐Guanidine Thiourea Dihydrobromide Affects HeLa Cell Growth Hampering Tubulin Polymerization

et al. 2020

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Cancer is going to be the first cause of mortality worldwide in the 21th century. It is considered a multifactorial disease that results from the combined influence of many genetic aberrations, leading to abnormal cell proliferation. As microtubules are strongly implicated in cellular growth, they represent an important target for cancer treatment. The well-known microtubule-targeting agents (MTAs) including paclitaxel, colchicine and vinca alkaloids are commonly used in the treatment of various cancers. However, adverse effects and drug resistance are major limitations in their clinical use. To find new candidates able to induce microtubule alteration with reduced toxic effects or drug resistance, we studied a small new series of derivatives that present imidazolinic, guanidinic, thioureidic and hydrazinic groups (1-9). All the compounds were tested for their antitumor activity against a panel of six tumoral cell models. In particular, compound 8 (nonane-1,9diyl-bis-S-amidinothiourea dihydrobromide) showed the lowest IC 50 value against HeLa cells, together with a low cytotoxicity for normal cells. This compound was able to induce the apoptotic mitochondrial pathway and inhibited tubulin polymerization with a similar efficacy to vinblastine and nocodazole. Taken together, these promising biological properties make compound 8 useful for the development of novel therapeutic approaches in cancer treatment.

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Correction: McLoughlin, E.C.; O’Boyle, N.M. Colchicine-Binding Site Inhibitors from Chemistry to Clinic: A Review. Pharmaceuticals 2020, 13, 8

Abstract: We, the authors, wish to make the following corrections to our paper [...]

Cited by 51 publications

References 2 publications

Evaluation of Colchicine’s interaction with the ATP-binding region of mice NLRP3-NACHT domain using molecular docking and dynamics simulation

Evaluation of Colchicine’s interaction with the ATP-binding region of mice NLRP3-NACHT domain using molecular docking and dynamics simulation

Structural insights into targeting of the colchicine binding site by ELR510444 and parbendazole to achieve rational drug design

α–ω Alkenyl‐bis‐S‐Guanidine Thiourea Dihydrobromide Affects HeLa Cell Growth Hampering Tubulin Polymerization

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