@article{3020799,
    title = "Design synthesis and evaluation of novel aldose reductase inhibitors: The case of indolyl–sulfonyl–phenols",
    author = "Koutsopoulos, K. and Lavrentaki, V. and Antoniou, I. and Kousaxidis, A. and Lefkopoulou, M. and Tsantili-Kakoulidou, A. and Kovacikova, L. and Stefek, M. and Nicolaou, I.",
    journal = "BIOORGANIC AND MEDICINAL CHEMISTRY",
    year = "2020",
    volume = "28",
    number = "15",
    publisher = "Elsevier Ireland Ltd",
    issn = "0968-0896",
    doi = "10.1016/j.bmc.2020.115575",
    keywords = "2 [(1h indol 1 yl)sulfonyl]phenol;  2 [(1h indol 2 yl)sulfonyl]phenol;  2 [(1h indol 3 yl)sulfonyl]phenol;  2 [(2 methoxyphenyl)sulfonyl] 1h indole;  3 [(2 methoxyphenyl)sulfonyl] 1h indole;  4 [(1h indol 1 yl)sulfonyl] 2 fluorophenol;  4 [(1h indol 1 yl)sulfonyl]phenol;  4 [(1h indol 2 yl)sulfonyl]phenol;  4 [(1h indol 3 yl)sulfonyl]phenol;  aldose reductase inhibitor;  unclassified drug;  aldehyde reductase;  enzyme inhibitor;  indole derivative;  phenol derivative;  protein binding;  sulfone, animal tissue;  Article;  catalyst;  controlled study;  drug mechanism;  drug screening;  drug structure;  drug synthesis;  enzyme assay;  enzyme inhibition;  molecular docking;  nonhuman;  process optimization;  rat;  structure activity relation;  animal;  chemistry;  drug design;  enzyme active site;  metabolism;  synthesis, Aldehyde Reductase;  Animals;  Catalytic Domain;  Drug Design;  Enzyme Assays;  Enzyme Inhibitors;  Indoles;  Molecular Docking Simulation;  Phenols;  Protein Binding;  Rats;  Sulfones",
    abstract = "Therapeutic interventions with aldose reductase inhibitors appear to be a promising approach to major pathological conditions (i.e. neuropathy/angiopathy related to chronic hyperglycemia, chronic inflammation and cancer). Until now, the most potent aldose reductase inhibitors have been carboxylic acid derivatives, which poorly permeate biological membranes. In this work, continuing our previous works, we promote the bioisosteric replacement of the carboxylic acid moiety to make equally potent yet more druggable inhibitors. © 2020 Elsevier Ltd"
}