86312-75-6Relevant articles and documents
Preparation of monohydroxyphthalocyanines and their use in the synthesis of heteronuclear complexes
Tolbin, Alexander Yu.,Tomilova, Larisa G.
, p. 286 - 288 (2008)
A directed synthesis of monohydroxyphthalocyanines has been developed; using the phthalocyanine-O-subphthalocyanine complex as an example, it has been shown that they can be used as building blocks in syntheses of heteronuclear complexes.
Synthesis and self-assembly of phthalocyanine-tethered block copolymers
Aimi, Junko,Komura, Motonori,Iyoda, Tomokazu,Saeki, Akinori,Seki, Shu,Takeuchi, Masayuki,Nakanishi, Takashi
supporting information, p. 2484 - 2490 (2015/03/18)
A series of novel phthalocyanine (Pc)-tethered block copolymers, Pc-poly(methyl methacrylate)-block-polystyrene (Pc-PMMA-b-PS), with various molecular weights (number average molecular weight mass = 41, 66, 86 kg mol-1), were prepared by atom transfer radical polymerization and click chemistry. The structurally related Pc-tethered homopolymer, Pc-PMMA was also synthesized for comparison. Pc-PMMA forms homogeneous polymer films containing π-assemblies of the terminal Pc groups, whereas Pc-PMMA-b-PS self-assembles into a cylindrical morphology in which the Pc units show π-π interactions inside the confined PMMA cylinders. Such polymer designs have potential applications in optoelectronic devices. This journal is
Inhibition of monoamine oxidase by C5-substituted phthalimide analogues
Manley-King, Clarina I.,Bergh, Jacobus J.,Petzer, Jacobus P.
body text, p. 4829 - 4840 (2011/09/20)
Literature reports that isatin as well as C5- and C6-substituted isatin analogues are reversible inhibitors of human monoamine oxidase (MAO) A and B. In general, C5- and C6-substitution of isatin leads to enhanced binding affinity to both MAO isozymes compared to isatin and in most instances result in selective binding to the MAO-B isoform. Crystallographic and modeling studies suggest that the isatin ring binds to the substrate cavities of MAO-A and -B and is stabilized by hydrogen bond interactions between the NH and the C2 carbonyl oxygen of the dioxoindolyl moiety and water molecules present in the substrate cavities of MAO-A and -B. Based on these observations and the close structural resemblances between isatin and its phthalimide isomer, a series of phthalimide analogues were synthesized and evaluated as MAO inhibitors. While phthalimide and N-aryl-substituted phthalimides were found to be weak MAO inhibitors, phthalimide homologues containing C5 substituents were potent reversible inhibitors of recombinant human MAO-B with IC50 values ranging from 0.007 to 2.5 μM and moderately potent reversible inhibitors of recombinant human MAO-A with IC50 values ranging from 0.22 to 9.0 μM. By employing molecular docking the importance of hydrogen bonding between the active sites of MAO-A and -B and the phthalimide inhibitors are highlighted.
