17371-59-4Relevant articles and documents
A Star-Shaped Triazine-Based Vitamin B5 Copper(II) Nanocatalyst for Tandem Aerobic Synthesis of Bis(indolyl)methanes
Hasanpour, Benyamin,Jafarpour, Maasoumeh,Eskandari, Ameneh,Rezaeifard, Abdolreza
, p. 4122 - 4129 (2020)
In this work, the catalytic efficiency of a novel bio-relevant triazine (TA)-based pantothenate (vitamin B5) copper(II) complex [Cu(II)-TA/B5] in the aerobic oxidation of benzyl alcohols and tandem synthesis of bis(indolyl)methanes was exploited. The star-shaped catalyst was characterized by different techniques such as FT-IR, EDX, ICP, TEM, and TGA. TEM images revealed a honeycomb structure resulting from the accumulation of nanoparticles with size ranging between 2–6 nm. The high yields and excellent selectivity were obtained for the production of various benzaldehydes and bis(indolyl)methanes under aerobic conditions. Recycling tests, spectroscopic data, and leaching experiments testified that the title heterogeneous bio-relevant catalyst preserved its activity and structural integrity during oxidation and coupling reactions. The presented catalytic systems qualify all requirements for efficient catalytic systems for applied goals.
Application of natural kaolin supported sulfuric acid as an ecofriendly catalyst for the efficient synthesis of bis(indolyl)methanes
Gordi, Zinat,Eshghi, Shaghayegh,Eshghi, Shohreh
, p. 905 - 908 (2012)
The acidified kaolin with sulfuric acid (2% w/w) is introduced as a novel, mild, highly efficient, easily prepared, very cheap, recyclable and ecofriendly catalyst in organic synthesis. This catalyst has been used successfully for the synthesis of bis(ind
Amberlyst-catalyzed reaction of indole: Synthesis of bisindolylalkane
Ke, Bowen,Qin, Yong,Wang, Yin,Wang, Fengpeng
, p. 1209 - 1212 (2005)
Amberlyst was found to be an effective catalyst for the condensation reactions of indoles 2 with aldehydes 3 to afford bisindolylalkanes 1 in good to excellent yields. Copyright Taylor & Francis, Inc.
Efficient RuIII-catalyzed condensation of indoles and aldehydes or ketones
Tabatabaeian, Khalil,Mamaghani, Manouchehr,Mahmoodi, Nosratollah,Khorshidi, Alireza
, p. 1541 - 1545 (2006)
Synthesis of bis(indolyl)methanes through condensation of indoles and various aldehydes or ketones, using RuIII as catalyst, is reported. It was found that the catalytic system involving RuIII affords the products smoothly under very
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Kamal,A.,Qureshi,A.A.
, p. 513 - 520 (1963)
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Sulfonated Tetraphenylethylene-Based Hypercrosslinked Polymer as a Heterogeneous Catalyst for the Synthesis of Symmetrical Triarylmethanes via a Dual C-C Bond-Cleaving Path
Kalita, Gitumoni,Deka, Namrata,Paul, Dipankar,Thapa, Loknath,Dutta, Gitish K.,Chatterjee, Paresh Nath
supporting information, p. 304 - 308 (2020/12/14)
A sulfonic acid functionalized tetraphenylethylene-based hypercrosslinked polymer (THP-SO 3H) with a well-developed porous network and accessible sulfonic acid sites was synthesized and characterized by different analytical techniques. The cata
Bis-indolylation of aldehydes and ketones using silica-supported FeCl3: Molecular docking studies of bisindoles by targeting SARS-CoV-2 main protease binding sites
Deb, Barnali,Debnath, Sudhan,Chakraborty, Ankita,Majumdar, Swapan
, p. 30827 - 30839 (2021/11/19)
We report herein an operationally simple, efficient and versatile procedure for the synthesis of bis-indolylmethanes via the reaction of indoles with aldehydes or ketones in the presence of silica-supported ferric chloride under grindstone conditions. The prepared supported catalyst was characterized by SEM and EDX spectroscopy. The present protocol has several advantages such as shorter reaction time, high yield, avoidance of using harmful organic solvents during the reaction and tolerance of a wide range of functional groups. Molecular docking studies targeted toward the binding site of SARS-CoV-2 main protease (3CLpro or Mpro) enzymes were investigated with the synthesized bis-indoles. Our study revealed that some of the synthesized compounds have potentiality to inhibit the SARS-CoV-2 Mpro enzyme by interacting with key amino acid residues of the active sites via hydrophobic as well as hydrogen bonding interactions.
