Novel 2-aminopyridine liganded Pd(II) N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure and bioactivity properties

Erdemir, Fatoş; Celepci, Duygu Barut; Aktaş, Aydın; Gök, Yetkın; Kaya, Rüya; Taslimi, Parham; Demir, Yeliz; Gülçın, İlhami

doi:10.1016/j.bioorg.2019.103134

Cited by 143 publications

(65 citation statements)

References 92 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed, this is a basic physiological reaction that underpins plenty of essential cellular mechanisms, like acid-base regulation, electrolyte secretion, respiration, bone resorption, calcification, and biosynthetic processes. [5][6][7][8] Therefore, many of the CAs are important drug targets for many pharmacological applications including the treatment of glaucoma, epilepsy, diuretics, and obesity, and more recently, they have been used as antitumor agents. Among the 16 different CA isoforms that have been isolated up to now, the cytosolic isoform hCA I is involved in retinal and cerebral edema, and the other physiologically related cytosolic isoform hCA II is associated with glaucoma, epilepsy, and edema.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, characterization, biological evaluation, and in silico studies of novel 1,3‐diaryltriazene‐substituted sulfathiazole derivatives

Işık

Akocak

Lolak

et al. 2020

Archiv der Pharmazie

Self Cite

View full text Add to dashboard Cite

In the present study, a series of eleven novel 1,3‐diaryltriazene‐substituted sulfathiazole moieties (ST1–11) was synthesized by the reaction of diazonium salt of sulfathiazole with substituted aromatic amines and their chemical structures were characterized by Fourier transform infrared, 1H‐NMR (nuclear magnetic resonance), 13C‐NMR, and high‐resolution mass spectroscopy methods. These synthesized novel derivatives were found to be effective inhibitor molecules for α‐glycosidase (α‐GLY), human carbonic anhydrase (hCA), and acetylcholinesterase (AChE), with KI values in the range of 426.84 ± 58.42–708.61 ± 122.67 nM for α‐GLY, 450.37 ± 50.35–1,094.34 ± 111.37 nM for hCA I, 504.37 ± 57.22–1,205.36 ± 195.47 nM for hCA II, and 68.28 ± 10.26–193.74 ± 19.75 nM for AChE. Among the synthesized novel compounds, several lead compounds were investigated against the tested metabolic enzymes. More specifically, ST11 (4‐[3‐(perfluorophenyl)triaz‐1‐en‐1‐yl]‐N‐(thiazol‐2‐yl)benzenesulfonamide) showed a highly efficient inhibition profile against hCA I, hCA II, and AChE, with KI values of 450.37 ± 50.35, 504.37 ± 57.22, and 68.28 ± 10.26 nM, respectively. Due to its significant biological inhibitory potency, this derivative may be considered as an interesting lead compound against these enzymes.

show abstract

Section: Introductionmentioning

confidence: 99%

Synthesis, characterization, biological evaluation, and in silico studies of novel 1,3‐diaryltriazene‐substituted sulfathiazole derivatives

Işık

Akocak

Lolak

et al. 2020

Archiv der Pharmazie

Self Cite

View full text Add to dashboard Cite

show abstract

“…In another study, novel 2‐aminopyridine liganded Pd(II) N‐heterocyclic carbene complexes were synthesized and tested inhibitory effects towards some methabolic enzymes such as α‐glycosidase, hCA I and II isoforms, butyrylcholinesterase, aldose reductase, and AChE. These compounds showed potent inhibion impact studied enzymes . In a recent study, novel sulfonamide‐hydrazone derivatives were synthesized to study their inhibition effect on hCA isoenzymes.…”

Section: Resultsmentioning

confidence: 99%

New Isoindole‐1,3‐dione Substituted Sulfonamides as Potent Inhibitors of Carbonic Anhydrase and Acetylcholinesterase: Design, Synthesis, and Biological Evaluation

et al. 2019

Self Cite

View full text Add to dashboard Cite

Herein, a series of isoindole‐1,3‐dione substituted sulfonamide derivatives (3, 4 a–k) were designed, synthesized, and biologically evaluated, as inhibitors of carbonic anhydrase (CA) and acetylcholinesterase (AChE). CA and AChE inhibitory activities of newly synthesized isoindole‐1,3‐dione substituted sulfonamides compounds (3, 4 a–k) towards the hCA I, II, and AChE were evaluated utilizing the Verpoorte's and Ellman's assays and checked against that of standard inhibitors, acetazolamide (AAZ) and tacrine (TAC). The developed compounds (3, 4 a–k) showed the potent hCA isoenzyme inhibitory effect with Ki constants ranging from 7.96 to 48.34 nM, compared to AAZ (Kis; 436.20 nM for hCA I and 93.53 nM for hCA II). Among these derivatives; 1,3‐dioxo‐1,3‐dihydroisobenzofuran‐5‐carbocyclic acid (3) and benzyl‐1,3‐dioxo‐2‐(4‐sulfomophenyl)isoindoline‐5‐carboxylate (4 i) determined to be effective AChE inhibitors (Kis, 103.51 and 108.92 nM, respectively); these compounds were almost as potent to TAC (Ki, 109.75 nM). Furthermore, molecular docking studies of derivatives 3 and 4 i were carried out utilizing the crystal structures of hCA I (PDB Code: 4WR7), II (PDB Code: 4HT0) isozymes and AChE (PDB Code: 4EY7) receptors to study their binding interactions.

show abstract

“…Before initiation of inhibition studies, both hCA activities were optimized in according to the literature . For this purpose, both hCA isoenzymes were studied under the optimum temperature (25°C) and optimum pH (p7.4) .…”

Section: Resultsmentioning

confidence: 99%

Synthesis of novel bis‐sulfone derivatives and their inhibition properties on some metabolic enzymes including carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase

Biçer

Kaya

Anil

et al. 2019

J Biochem & Molecular Tox

View full text Add to dashboard Cite

In this study, a series of novel bis-sulfone compounds (2a-2j) were synthesized by oxidation of the bis-sulfides under mild reaction conditions. The bis-sulfone derivatives were characterized by 1 H-NMR, 13 C-NMR, Fourier-transform infrared spectroscopy, and elemental analysis techniques. Nuclear Overhauser effect experiments were performed to determine the orientation of the sulfonyl groups in bis-sulfone derivatives. Here, we report the synthesis and testing of novel bis-sulfone compound-based hybrid scaffold of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors for the development of novel molecules toward the therapy of Alzheimer's disease. The novel synthesized bis-sulfone compounds demonstrated K i values between 11.4 ± 3.4 and 70.7 ± 23.2 nM on human carbonic anhydrase I isozyme (hCA I), 28.7 ± 6.6 to 77.6 ± 5.6 nM on human carbonic anhydrase II isozyme (hCA II), 18.7 ± 2.61 to 95.4 ± 25.52 nM on AChE, and 9.5 ± 2.1 to 95.5 ± 1.2 nM on BChE enzymes. The results showed that novel bissulfone derivatives can have promising drug potential for glaucoma, leukemia, epilepsy, and Alzheimer's disease, which are associated with the high enzymatic activity of hCA I, hCA II, AChE, and BChE enzymes. K E Y W O R D S acetylcholinesterase, bis-sulfide, butyrylcholinesterase, bis-sulfone, carbonic anhydrase

show abstract

Novel 2-aminopyridine liganded Pd(II) N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure and bioactivity properties

Cited by 143 publications

References 92 publications

Synthesis, characterization, biological evaluation, and in silico studies of novel 1,3‐diaryltriazene‐substituted sulfathiazole derivatives

Synthesis, characterization, biological evaluation, and in silico studies of novel 1,3‐diaryltriazene‐substituted sulfathiazole derivatives

New Isoindole‐1,3‐dione Substituted Sulfonamides as Potent Inhibitors of Carbonic Anhydrase and Acetylcholinesterase: Design, Synthesis, and Biological Evaluation

Synthesis of novel bis‐sulfone derivatives and their inhibition properties on some metabolic enzymes including carbonic anhydrase, acetylcholinesterase, and butyrylcholinesterase

Contact Info

Product

Resources

About