Discovery of novel benzenesulfonamides incorporating 1,2,3-triazole scaffold as carbonic anhydrase I, II, IX, and XII inhibitors

Buza, Aida; Türkeş, Cüneyt; Arslan, Mustafa; Demir, Yeliz; Dinçer, Büşra; Nixha, Arleta Rifati; Beydemır, Şükrü

doi:10.1016/j.ijbiomac.2023.124232

Cited by 36 publications

(10 citation statements)

References 82 publications

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“…The Small‐Molecule Drug Discovery Suite 2022–3 for Mac (Schrödinger, LLC, NY, USA) was utilized to conduct in silico molecular docking study, as previously reported [41,42] . This suite includes the Maestro, Protein Preparation Wizard, [43,44] SiteMap, [45] LigPrep, [46] Receptor Grid Generation, [47] Ligand Docking, [48] and Prime MM‐GBSA [49,50] tools. The Protein Data Bank (http://www.rcsb.org/) was utilized to acquire the crystal structure of LPO (PDB ID: 3UBA, Resolution: 2.65).…”

Section: Methodsmentioning

confidence: 99%

Screening of in Vitro Inhibition of Lactoperoxidase Enzyme by Methyl Benzoate Derivatives with Molecular Docking Studies

Abul

Gerni

Korkmaz

et al. 2023

Chemistry & Biodiversity

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Lactoperoxidase enzyme (LPO) is secreted from salivary, mammary, and other mucosal glands including the bronchi, lungs, and nose, which had functions as a natural and the first line of defense towards viruses and bacteria. In this study, methyl benzoates were examined in LPO enzyme activity. Methyl benzoates are used as precursors in the synthesis of aminobenzohydrazides used as LPO inhibitors. For this purpose, LPO was purified in a single step using sepharose‐4B‐l‐tyrosine‐sulfanilamide affinity gel chromatography with a yield of 9.91 % from cow milk. Also, some inhibition parameters including the half maximal inhibitory concentration (IC50) value and an inhibition constant (Ki) values of methyl benzoates were determined. These compounds inhibited LPO with Ki values ranging from 0.033±0.004 to 1540.011±460.020 μM. Compound 1 a (methyl 2‐amino‐3‐bromobenzoate) showed the best inhibition (Ki=0.033±0.004 μM). The most potent inhibitor (1 a) showed with a docking score of −3.36 kcal/mol and an MM‐GBSA value of −25.05 kcal/mol, of these methyl benzoate derivatives (1 a–16 a) series are established H‐bond within the binding cavity with residues Asp108 (distance of 1.79 Å), Ala114 (distance of 2.64 Å), and His351 (distance of 2.12 Å).

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Section: Methodsmentioning

confidence: 99%

Screening of in Vitro Inhibition of Lactoperoxidase Enzyme by Methyl Benzoate Derivatives with Molecular Docking Studies

Abul

Gerni

Korkmaz

et al. 2023

Chemistry & Biodiversity

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“…Maestro [66] was utilized to produce molecular docking images. Also, ADME/T properties of the derivatives ( SG1 – 13 ) were calculated using the Qikprop tool [67] …”

Section: Methodsmentioning

confidence: 99%

Synthesis and Characterization of Novel 1,3‐Diaryltriazene‐Substituted Sulfaguanidine Derivatives as Selective Carbonic Anhydrase Inhibitors: Biological Evaluation, in Silico ADME/T and Molecular Docking Study

Akocak

Lolak

Duran

et al. 2023

Chemistry & Biodiversity

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Sulfonamide compounds known as human carbonic anhydrase (hCA) inhibitors are used in the treatment of many diseases such as epilepsy, antibacterial, glaucoma, various diseases. 1,3‐diaryl‐substituted triazenes and sulfaguanidine are used for therapeutic purposes in many drug structures. Based on these two groups, the synthesis of new compounds is important. In the present study, the novel 1,3‐diaryltriazene‐substituted sulfaguanidine derivatives (SG1‐13) were synthesized and fully characterized by spectroscopic and analytic methods. Inhibitory effect of these compounds on the hCA I and hCA II was screened as in vitro. All the series of synthesized compounds have been identified as potential hCA isoenzymes inhibitory with KI values in the range of 6.44±0.74‐86.85±7.01 nM for hCA I and with KI values in the range of 8.16±0.40‐77.29±9.56 nM for hCA II. Moreover, the new series of compounds showed a more effective inhibition effect than the acetazolamide used as a reference. The possible binding positions of the compounds with a binding affinity to the hCA I and hCA II was demonstrated by in silico studies. In conclusion, compounds with varying degrees of affinity for hCA isoenzymes have been designed and as selective hCA inhibitors. These compounds may be potential alternative agents that can be used to treat or prevent diseases associated with glaucoma and hCA inhibition.

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“…The Small‐Molecule Drug Discovery Suite 2023–2 for Mac was employed, which included various modules such as Maestro, LigPrep, [63] Protein Preparation Wizard, [64] SiteMap, [65] Receptor Grid Generation, [66] and Glide Ligand Docking [63] . To begin, the chemical structure of Puerarin was obtained from a chemical database (PubChem CID 5281807) and was subsequently processed with the LigPrep software [67] . Additionally, the crystal structures of two enzymes, AChE [53] and BChE [54] (PDB codes of 7XN1 and 4BDS, respectively), were obtained from the Protein Data Bank [68] and optimized using the Protein Preparation Wizard tool [69] .…”

Section: Methodsmentioning

confidence: 99%

“…[63] To begin, the chemical structure of Puerarin was obtained from a chemical database (PubChem CID 5281807) and was subsequently processed with the LigPrep software. [67] Additionally, the crystal structures of two enzymes, AChE [53] and BChE [54] (PDB codes of 7XN1 and 4BDS, respectively), were obtained from the Protein Data Bank [68] and optimized using the Protein Preparation Wizard tool. [69] This was done using the force field OPLS4, [70] with default parameters set at pH 7.4 � 0.5.…”

Section: In Silico Studymentioning

confidence: 99%

Determination of the Antioxidant Capacity of Puerarin and Its Effect on Cholinesterases by in vitro and in silico Methods

İnan Ergün,

Topal

2023

ChemistrySelect

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Puerarin, which was used as a natural isoflavone in this study, was obtained from the Kudzu plant. The inhibitory effect of puerarin on acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes was investigated. The IC50 values of AChE (177.73 nM) and BChE (315.07 nM) were determined. The binding mechanism of puerarin, which has a high inhibitory effect on the active site of the enzyme, was demonstrated by the molecular docking method. The antioxidant activity was evaluated for the same molecule. For this purpose, Fe3+‐Fe2+ reducing capacity, ABTS radical scavenging activity, CUPRAC method, DPPH⋅ scavenging activity and DMPD radical scavenging method were used. The percentage (%) inhibition amount of puerarin molecule was calculated as 99.33 % for ABTS radical scavenging activity, which is the more preferred method for natural products. The absorbtion value of iron reduction of Puerarin was 0.122±0.010, and the value of copper reduction was 0.633±0.026. Our research efforts include uncovering the potent antioxidant potential of puerarin and, simultaneously, a comparative study of tacrine, primarily emphasizing its inhibitory effects against AChE and BChE enzymes. The puerarin is expected to be a guide for drug discovery against many problems, especially oxidative cell damage in Alzheimer's disease, mitochondrial dysfunction (MD), cancer, and cardiovascular diseases.

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Discovery of novel benzenesulfonamides incorporating 1,2,3-triazole scaffold as carbonic anhydrase I, II, IX, and XII inhibitors

Cited by 36 publications

References 82 publications

Screening of in Vitro Inhibition of Lactoperoxidase Enzyme by Methyl Benzoate Derivatives with Molecular Docking Studies

Screening of in Vitro Inhibition of Lactoperoxidase Enzyme by Methyl Benzoate Derivatives with Molecular Docking Studies

Synthesis and Characterization of Novel 1,3‐Diaryltriazene‐Substituted Sulfaguanidine Derivatives as Selective Carbonic Anhydrase Inhibitors: Biological Evaluation, in Silico ADME/T and Molecular Docking Study

Determination of the Antioxidant Capacity of Puerarin and Its Effect on Cholinesterases by in vitro and in silico Methods

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