Synthesis, characterization and biological activity evaluation of novel naphthalenylmethylen hydrazine derivatives as carbonic anhydrase inhibitors


Shirinzadeh H., Dilek E.

JOURNAL OF MOLECULAR STRUCTURE, vol.1220, 2020 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 1220
  • Publication Date: 2020
  • Doi Number: 10.1016/j.molstruc.2020.128657
  • Journal Name: JOURNAL OF MOLECULAR STRUCTURE
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chimica, Compendex, INSPEC
  • Keywords: Carbonic anhydrase, Enzyme inhibition, Naphthalenylmethylen hydrazine, Synthesis, IN-VITRO INHIBITION, THERAPEUTIC APPLICATIONS, SCHIFF, ISOZYMES, ENZYMES, BINDING, BASES
  • Erzincan Binali Yildirim University Affiliated: Yes

Abstract

In the current study some derivatives of naphthalenylmethylen hydrazine were synthesized and possible in vitro hCA I and II enzymes inhibition effects were investigated. The designed compounds were synthesized by condensation of phenylhydrazine with 1-naphthaldehyde or 6-methoxy-2-naphthaldehyde and eight compounds (1a-h) were obtained. The novel Schiff bases derivatives (compounds 1a-1h) were effective inhibitors of the cytosolic carbonic anhydrase I and II isoforms (hCA I and II) with Ki values in the range of 80.60 +/- 17.90 to 492.53 +/- 95.23 nM for hCA I, 102.88 +/- 18.44 to 461.09 +/- 102.50 nM for hCA II. lf compound shows a remarkable inhibitory effect of hCA I and hCA II isoenzymes among the new synthesized compounds. The new derivatives of naphthalenylmethylen hydrazine can be a potent inhibitor of both cytosolic CA isoenzymes which are commonly used in the pharmaceutical industries and medical areas. (C) 2020 Elsevier B.V. All rights reserved.