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Biophys Chem. 2021 Oct;277:106658. doi: 10.1016/j.bpc.2021.106658. Epub 2021 Jul 24.

Adenosine deaminase - A target for new piperazine derivatives.

Biophysical chemistry

Anahit Bakaryan, Luiza Karapetyan, Naira Hakobyan, Emidio Camaioni, Sona Mardanyan, Alvard Antonyan

Affiliations

  1. H. Buniatian Institute of Biochemistry of Armenian NAS, 5/1, P. Sevak Str., Yerevan 0014, Armenia.
  2. A.L. Mnjoyan Institute of Fine Organic Chemistry of Armenian NAS, 26 Azatutyan Ave., Yerevan 0014, Armenia.
  3. Department of Pharmaceutical Sciences, University of Perugia, via del Liceo, 1-06123 Perugia, Italy. Electronic address: [email protected].
  4. H. Buniatian Institute of Biochemistry of Armenian NAS, 5/1, P. Sevak Str., Yerevan 0014, Armenia. Electronic address: [email protected].

PMID: 34333397 DOI: 10.1016/j.bpc.2021.106658

Abstract

The level of adenosine deaminase (ADA) activity increases in pathological effusions. Therefore, the concentration of its substrate, anti-inflammatory adenosine, decreases, thereby aggravating inflammation. Hence, the quest for ADA inhibiting compounds is an actual problem in medicine and pharmacology. This work describes the inhibition of bovine ADA by new synthesized piperazine compounds. 15 compounds were screened; IC

Copyright © 2021. Published by Elsevier B.V.

Keywords: Adenosine deaminase isoforms; Enzyme inhibition; Fluorescence quenching; Molecular docking; Protein-ligand interaction

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