360784-23-2Relevant academic research and scientific papers
Molecular docking studies of (1E,3E,5E )-1,6-bis(substituted phenyl)-hexa-1,3,5-triene and 1,4-bis(substituted trans-styryl)benzene analogs as novel tyrosinase inhibitors
Ha, Young Mi,Lee, Hye Jin,Park, Daeui,Jeong, Hyoung Oh,Park, Ji Young,Park, Yun Jung,Lee, Kyung Jin,Lee, Ji Yeon,Moon, Hyung Ryong,Chung, Hae Young
, p. 55 - 65 (2013/03/14)
We simulated the docking of the tertiary structure of mushroom tyrosinase with our compounds. From the structure-tyrosinase inhibitory activity relationship, it is notable that compounds 4, 8 and 11 showed similar or better activity rates than kojic acid which was used as a positive control. Compounds 17, 21, and 23 among benzene analogs that possess the same substituent showed significantly lower tyrosinase inhibitory effects. Therefore, we have confirmed that among the compounds showing better tyrosinase inhibitory effects than kojic acid, the compounds with triene analogs have better tyrosinase inhibitory effect than the compounds with benzene analogs. Docking simulation suggested the mechanism of compounds by several key residues which had possible hydrogen bonding interactions. The pharmacophore model underlined the features of active compounds, 4,4′-((1E,3E,5E )-hexa-1,3,5-triene-1,6-diyl)diphenol, 5,5′-((1E,3E,5E )-hexa-1,3,5-triene-1,6-diyl)bis(2-methoxy-phenol), and 5,5′-((1 E,3E,5E )-hexa-1,3,5-triene-1,6-diyl)dibenzene-1,3-diol among triene derivatives which had several hydrogen bond groups on both terminal rings. The soundness of the docking results and the agreement with the pharmacophores suggest that it can be conveniently exploited to design inhibitors with an improved affinity for tyrosinase.
Phenolic bis-styrylbenzenes as β-amyloid binding ligands and free radical scavengers
Flaherty, Daniel P.,Kiyota, Tomomi,Dong, Yuxiang,Ikezu, Tsuneya,Vennerstrom, Jonathan L.
, p. 7992 - 7999 (2011/03/19)
Starting from bisphenolic bis-styrylbenzene DF-9 (4), β-amyloid (Aβ) binding affinity and specificity for phenolic bis-styrylbenzenes, monostyrylbenzenes, and alkyne controls were determined by fluorescence titration with β-amyloid peptide Aβ1-40 and a fluorescence assay using APP/PS1 transgenic mouse brain sections. Bis-styrylbenzene SAR is derived largely from work on symmetrical compounds. This study is the first to describe Aβ binding data for bis-styrylbenzenes unsymmetrical in the outer rings. With one exception, binding affinity and specificity were decreased by adding and/or changing the substitution pattern of phenol functional groups, changing the orientation about the central phenyl ring, replacing the alkene with alkyne bonds, or eliminating the central phenyl ring. The only compound with an Aβ binding affinity and specificity comparable to 4 was its 3-hydroxy regioisomer 8. Like 4, 8 crossed the blood-brain barrier and bound to Aβ plaques in vivo. By use of a DPPH assay, phenol functional groups with para orientations seem to be a necessary, but insufficient, criterion for good free radical scavenging properties in these compounds.
Bis-, tris-, and tetrakis(squaraines) linked by stilbenoid scaffolds
Gerold, Jürgen,Holzenkamp, Uta,Meier, Herbert
, p. 2757 - 2763 (2007/10/03)
The oligosquaraines 1-5, with stilbenoid scaffolds, were prepared by multistep syntheses in which the final steps consisted of condensation reactions between the semisquaric acid 21 and multiple resorcinols 12b-15b and 17b. The target compounds exhibit in
