Wadood A

References (13)

Title : Biologically Potent Benzimidazole-Based-Substituted Benzaldehyde Derivatives as Potent Inhibitors for Alzheimer's Disease along with Molecular Docking Study - Adalat_2023_Pharmaceuticals.(Basel)_16_
Author(s) : Adalat B , Rahim F , Rehman W , Ali Z , Rasheed L , Khan Y , Farghaly TA , Shams S , Taha M , Wadood A , Shah SAA , Abdellatif MH
Ref : Pharmaceuticals (Basel) , 16 : , 2023
Abstract : Twenty-one analogs were synthesized based on benzimidazole, incorporating a substituted benzaldehyde moiety (1-21). These were then screened for their acetylcholinesterase and butyrylcholinesterase inhibition profiles. All the derivatives except 13, 14, and 20 showed various inhibitory potentials, ranging from IC(50) values of 0.050 +/- 0.001 microM to 25.30 +/- 0.40 microM against acetylcholinesterase, and 0.080 +/- 0.001 microM to 25.80 +/- 0.40 microM against butyrylcholinesterase, when compared with the standard drug donepezil (0.016 +/- 0.12 microM and 0.30 +/- 0.010 microM, against acetylcholinesterase and butyrylcholinesterase, respectively). Compound 3 in both cases was found to be the most potent compound due to the presence of chloro groups at the 3 and 4 positions of the phenyl ring. A structure-activity relationship study was performed for all the analogs except 13, 14, and 20, further, molecular dynamics simulations were performed for the top two compounds as well as the reference compound in a complex with acetylcholinesterase and butyrylcholinesterase. The molecular dynamics simulation analysis revealed that compound 3 formed the most stable complex with both acetylcholinesterase and butyrylcholinesterase, followed by compound 10. As compared to the standard inhibitor donepezil both compounds revealed greater stabilities and higher binding affinities for both acetylcholinesterase and butyrylcholinesterase.
ESTHER : Adalat_2023_Pharmaceuticals.(Basel)_16_
PubMedSearch : Adalat_2023_Pharmaceuticals.(Basel)_16_
PubMedID: 37259358

Title : Para-Substituted Thiosemicarbazones as Cholinesterase Inhibitors: Synthesis, In Vitro Biological Evaluation, and In Silico Study - Khan_2023_ACS.Omega_8_5116
Author(s) : Khan M , Gohar H , Alam A , Wadood A , Shareef A , Ali M , Khalid A , Abdalla AN , Ullah F
Ref : ACS Omega , 8 :5116 , 2023
Abstract : The current research reports the synthesis of 14 para-substituted thiosemicarbazone derivatives in good to excellent yields using standard procedures. Initially, 4-ethoxybenzaldehyde (1) and 4-nitrobenzaldehyde (2) were refluxed with thiosemicarbazide in the presence of acetic acid in ethanol for 4-5 h. Then, various substituted phenacyl bromides were treated with the desired thiosemicarbazones (3 and 4) in the presence of triethylamine in ethanol with constant stirring for 5-6 h. The resulting derivatives were confirmed through electron impact mass spectrometry and (1)H NMR spectroscopy and evaluated for anticholinesterase inhibitory activity. Among the series, four compounds, 19, 17, 7, and 6, showed potent inhibitory activity against the acetylcholinesterase (AChE) enzyme, having IC(50) values of 110.19 +/- 2.32, 114.57 +/- 0.15, 140.52 +/- 0.11, and 160.04 +/- 0.02 microM, respectively, compared with standard galantamine (IC(50) = 104.5 +/- 1.20 microM). Similarly, compounds 19 (IC(50) = 145.11 +/- 1.03 microM), 9 (IC(50) = 147.20 +/- 0.09 microM), 17 (IC(50) = 150.36 +/- 0.18 microM), and 6 (IC(50) = 190.21 +/- 0.13 microM) were the most excellent inhibitors of butyrylcholinesterase (BChE) when compared with the standard drug galantamine (IC(50) = 156.8 +/- 1.50 microM). In silico studies were accomplished on the produced derivatives in order to explain the binding interface of compounds with the active sites of AChE and BChE enzymes.
ESTHER : Khan_2023_ACS.Omega_8_5116
PubMedSearch : Khan_2023_ACS.Omega_8_5116
PubMedID: 36777613

Title : Anti-Alzheimer and Antioxidant Effects of Nelumbo nucifera L. Alkaloids, Nuciferine and Norcoclaurine in Alloxan-Induced Diabetic Albino Rats - Khan_2022_Pharmaceuticals.(Basel)_15_1205
Author(s) : Khan S , Khan HU , Khan FA , Shah A , Wadood A , Ahmad S , Almehmadi M , Alsaiari AA , Shah FU , Kamran N
Ref : Pharmaceuticals (Basel) , 15 : , 2022
Abstract : The present study is aimed to determine the efficacy and dose response of the nuciferine (1), norcoclaurine (2) and crude extract of Nelumbo nucifera in managements of diabetes, Alzheimer disease and related allergies. Experimentally, alloxan (100 mg/kg body weight (b.w.))-induced diabetic rats (200-250 g) were divided into seven groups (n = 6). Group I: normal control, Group II: diabetic control, Group III: standard treated with glibenclamide and Group lV-VII: treated with methanolic crude extracts (100, 200 mg/kg), nuciferine and norcoclaurine (10 mg/kg b.w.) for 15 days. Different tests were performed, including blood glucose, body weights and antioxidant enzyme assays, i.e., superoxide dismutase (SOD), catalase test (CAT), lipid peroxidation assay (TBARS), glutathione assay (GSH) and acetylcholinesterase (AChE) assay. Nuciferine and norcoclaurine significantly reduced blood glucose (p < 0.05) and restored body weight in diabetic rats. Moreover, nuciferine and norcoclaurine (10 mg/kg) significantly recovered the antioxidant enzymes (SOD, CAT, GPx and GSH) which decreased during induced diabetes. Significant increase in TBARS was also observed in the diabetic group and nuciferine as well as norcoclaurine (10 mg/kg) inhibited the increase in TBARS in diabetic animals (p < 0.05), as compared to glibenclamide. AChE activity was significantly recovered by nuciferine and norcoclaurine (10 mg/kg) both in the blood and brain of the diabetic group (p < 0.05). Nuciferine and norcoclaurine showed potent inhibitory effects against alpha-glucosidase and alpha-amylase with IC(50), 19.06 +/- 0.03, 15.03 +/- 0.09 microM and 24.07 +/- 0.05, 18.04 +/- 0.021 microM, as confirmed by molecular docking studies. This study concludes that nuciferine and norcoclaurine significantly improve memory and could be considered as an effective phytomedicine for diabetes, Alzheimer's disease (AD) and oxidative stress.
ESTHER : Khan_2022_Pharmaceuticals.(Basel)_15_1205
PubMedSearch : Khan_2022_Pharmaceuticals.(Basel)_15_1205
PubMedID: 36297317

Title : In silico approaches to develop herbal acaricides against R. (Boophilus) Microplus and In vitro Anti-Tick activities of selected medicinal plants - Malak_2022_Saudi.J.Biol.Sci_29_103302
Author(s) : Malak N , Niaz S , Wadood A , Nasreen N , Ali I , Iqbal J , Swelum AA , Ezzat Ahmed A , Alkahtani MA , Zajac Z , Khan A
Ref : Saudi J Biol Sci , 29 :103302 , 2022
Abstract : In tropical and sub-tropical areas of the world the most damaging pest of the livestock sector are cattle tick, Rhipicephalus microplus. The current study was aimed to generate phytochemical derived acaricides to control Rhipicephalus microplus populations, to maintain livestock herd production, minimize economic losses and to reduce uses of man-made chemicals acaricides. To achieve this goal, Adult immersion and larval package test were used to determine the feasibility of Berberium lyceum and Tamarixa aphylla against Rhipicephalus microplus ticks. Further, an In silico technique was employed to discover biologically active substances from both plants using docking method. Berberium lyceum and Tamarixa aphylla exhibited a reasonably high fatal effect at 40.0 mg/L on egg laying (index of egg laying = 0.19 and 0.19) respectively, thus inhibiting the oviposition (49.5 and 45.1, respectively) and the larval mortality (97% and 93%, respectively). Further, we also used Chem-Draw ultra-software (v. 12.0.2.1076. 2010) to illustrate different structures of38 known bioactive phytochemicals which are discovered in the PubChem database and verify the hypothesis that tick inhibition was linked to acetylcholinesterase (AChE). Barbamunine and rutin from Berberium lyceum showed remarkable interaction with RmAChE1 active site residues with docking scores of -9.11 to -8.71 while phytol and dehydrodigallic acid from Tamarix aphylla showed comparable docking scores of -7.17 and -7.14 respectively against Rhipicephalus microplus acetylcholinesterase protein. Based on obtained result, we believe that Berberium lyceum and Tamarixa aphylla bioactive components could be potential candidates in the control and management of Rhipicephalus microplus and should be studied further as a supplement or replacement for synthetic acaricides.
ESTHER : Malak_2022_Saudi.J.Biol.Sci_29_103302
PubMedSearch : Malak_2022_Saudi.J.Biol.Sci_29_103302
PubMedID: 35602870

Title : New bis-thiazolidinone based chalcone analogues as effective inhibitors of Alzheimer's disease: Synthesis, molecular docking, acetylcholinesterase and butyrylcholinesterase study - Hussain_2022_Chem.Biodivers__
Author(s) : Hussain R , Rahim F , Rehman W , Taha M , Khan S , Zaman K , Ali Shah SA , Wadood A , Imran S , Abdellatif M
Ref : Chem Biodivers , : , 2022
Abstract : A series of twenty bis -thiazolidinone based chalcone scaffolds (1-20) were synthesized and characterized by using various spectroscopic tools such as HR-EI-MS, 1 HNMR, 13 CNMR and were screened in vitro for their AChE and BuChE inhibition profile. It was noteworthy, that all the synthetic analogues (except analogues 10, 12 and 1 4 , which are found to be inactive) showed moderate to good inhibitory potentials on screening against AchE and BuChE enzymes with IC 50 values ranging from 0.10 +/-0.050 to 7.60 +/- 0.10 microM and 0.10 +/- 0.050microM to 10.70 +/- 0.20 microM as compared to standard Donepezil inhibitor (IC 50 = 0.016 +/- 0.12 microM), (IC 50 = 4.5 +/- 0.11 microM). Among the current series, analogue 20 (IC 50 = 0.10 +/- 0.050microM), (IC 50 = 0.10 +/- 0.050microM) bearing trihydroxy substitutions on ortho -, meta - and para -position of both rings A and B , respectively was found to be the most active inhibitor of AChE and BuChE enzymes . Analogue 19 (IC 50 = 0.20 +/- 0.050 microM), (IC 50 = 0.20 +/- 0.050microM) bearing dihydroxy substitutions on ortho - and meta -position of both ring A and ring B respectively, was identified as the second most potent inhibitor against both these enzymes. Potent analogs were further subjected to molecular docking study to identify the binding interactions with enzymes active site. SAR study was done for all the analogues mostly based on substitution pattern on both ring A and B respectively.
ESTHER : Hussain_2022_Chem.Biodivers__
PubMedSearch : Hussain_2022_Chem.Biodivers__
PubMedID: 35997224

Title : Synthesis of indole derivatives as Alzheimer inhibitors and their molecular docking study - Homoud_2022_J.Biomol.Struct.Dyn__1
Author(s) : Homoud ZA , Taha M , Rahim F , Iqbal N , Nawaz M , Farooq RK , Wadood A , Alomari M , Islam I , Algheribe S , Rehman AU , Khan KM , Uddin N
Ref : J Biomol Struct Dyn , :1 , 2022
Abstract : Acetylcholinesterase prevails in the healthy brain, with butyrylcholinesterase reflected to play a minor role in regulating brain acetylcholine (ACh) levels. However, BuChE activity gradually increases in patients with (AD), while AChE activity remains unaffected or decays. Both enzymes therefore represent legitimate therapeutic targets for ameliorating the cholinergic deficit considered to be responsible for the declines in cognitive, behavioural, and global functioning characteristic of AD. Current study described the synthesis of indole-based sulfonamide derivatives (1-23) and their biological activity. Synthesis of these scaffolds were achieved by mixing chloro-substituted indole bearing amine group with various substituted benzene sulfonyl chloride in pyridine, under refluxed condition to obtained desired products. All products were then evaluated for AchE and BuchE inhibitory potential compare with positive Donepezil as standard drug for both AchE and BchE having IC(50) = 0.016 0.12 and 0.30 0.010 M respectively. In this regard analog 9 was found potent having IC(50) value 0.15 0.050 M and 0.20 0.10 for both AchE and BuChE respectively. All other derivatives also found with better potential. All compounds were characterized by various techniques such as (1)H, (13)C-NMR and HREI-MS. In addition, biological activity was maintained to explore the bioactive nature of scaffolds and their protein-ligand interaction (PLI) was checked through molecular docking study.Communicated by Ramaswamy H. Sarma.
ESTHER : Homoud_2022_J.Biomol.Struct.Dyn__1
PubMedSearch : Homoud_2022_J.Biomol.Struct.Dyn__1
PubMedID: 36404604

Title : Synthesis, in vitro biological screening and docking study of benzo[d]oxazole bis Schiff base derivatives as a potent anti-Alzheimer agent - Taha_2022_J.Biomol.Struct.Dyn__1
Author(s) : Taha M , Rahim F , Zaman K , Anouar EH , Uddin N , Nawaz F , Sajid M , Khan KM , Shah AA , Wadood A , Rehman AU , Alhibshi AH
Ref : J Biomol Struct Dyn , :1 , 2022
Abstract : We have synthesized benzo[d]oxazole derivatives (1-21) through a multistep reaction. Alteration in the structure of derivatives was brought in the last step via using various substituted aromatic aldehydes. In search of an anti-Alzheimer agent, all derivatives were evaluated against acetylcholinesterase and butyrylcholinesterase enzyme under positive control of standard drug donepezil (IC(50) = 0.016 +/- 0.12 and 4.5 +/- 0.11 microM) respectively. In case of acetylcholinesterase enzyme inhibition, derivatives 8, 9 and 18 (IC(50) = 0.50 +/- 0.01, 0.90 +/- 0.05 and 0.3 +/- 0.05 microM) showed very promising inhibitory potentials. While in case of butyrylcholinesterase enzyme inhibition, most of the derivatives like 6, 8, 9, 13, 15, 18 and 19 (IC(50) = 2.70 +/- 0.10, 2.60 +/- 0.10, 2.20 +/- 0.10, 4.25 +/- 0.10, 3.30 +/- 0.10, 0.96 +/- 0.05 and 3.20 +/- 0.10 microM) displayed better inhibitory potential than donepezil. Moreover, derivative 18 is the most potent one among the series in both inhibitions. The binding interaction of derivatives with the active gorge of the enzyme was confirmed via a docking study. Furthermore, the binding interaction between derivatives and the active site of enzymes was correlated through the SAR study. Structures of all derivatives were confirmed through spectroscopic techniques such as (1)H-NMR, (13)C-NMR and HREI-MS, respectively.Communicated by Ramaswamy H. Sarma.
ESTHER : Taha_2022_J.Biomol.Struct.Dyn__1
PubMedSearch : Taha_2022_J.Biomol.Struct.Dyn__1
PubMedID: 34989316

Title : Comparative Cholinesterase, alpha-Glucosidase Inhibitory, Antioxidant, Molecular Docking, and Kinetic Studies on Potent Succinimide Derivatives - Ahmad_2020_Drug.Des.Devel.Ther_14_2165
Author(s) : Ahmad A , Ullah F , Sadiq A , Ayaz M , Saeed Jan M , Shahid M , Wadood A , Mahmood F , Rashid U , Ullah R , Sahibzada MUK , Alqahtani AS , Mahmood HM
Ref : Drug Des Devel Ther , 14 :2165 , 2020
Abstract : Introduction: The current study was designed to synthesize derivatives of succinimide and compare their biological potency in anticholinesterase, alpha-glucosidase inhibition, and antioxidant assays. Methods: In this research, two succinimide derivatives including (S)-1-(2,5-dioxo-1-phenylpyrrolidin-3-yl) cyclohexanecarbaldehyde (Compound 1) and (R)-2-((S)-2,5-dioxo-1-phenylpyrrolidin-3-yl)-2-phenylpropanal (Compound 2) were synthesized using Michael addition. Both the compounds, ie, 1 and 2 were evaluated for in-vitro acetylcholinesterase (AChE), butyrylctcholinesterase (BChE), antioxidant, and alpha-glucosidase inhibitory potentials. Furthermore, molecular docking was performed using Molecular Operating Environment (MOE) to explore the binding mode of both the compounds against different enzymes. Lineweaver-Burk plots of enzyme inhibitions representing the reciprocal of initial enzyme velocity versus the reciprocal of substrate concentration in the presence of synthesized compounds and standard drugs were constructed using Michaelis-Menten kinetics. Results: In AChE inhibitory assay, compounds 1 and 2 exhibited IC50 of 343.45 and 422.98 microM, respectively, against AChE enzyme. Similarly, both the compounds showed IC50 of 276.86 and 357.91 microM, respectively, against BChE enzyme. Compounds 1 and 2 displayed IC50 of 157.71 and 471.79 microM against alpha-glucosidase enzyme, respectively. In a similar pattern, compound 1 exhibited to be more potent as compared to compound 2 in all the three antioxidant assays. Compound 1 exhibited IC50 values of 297.98, 332.94, and 825.92 microM against DPPH, ABTS, and H2O2 free radicals, respectively. Molecular docking showed a triple fold in the AChE and BChE activity for compound 1 compared with compound 2. The compound 1 revealed good interaction against both the AChE and BChE enzymes which revealed the high potency of this compound compared to compound 2. Conclusion: Both succinimide derivatives exhibited considerable inhibitory activities against cholinesterases and alpha-glucosidase enzymes. Of these two, compound 1 revealed to be more potent against all the in-vitro targets which was supported by molecular docking with the lowest binding energies. Moreover, compound 1 also proved to have antiradical properties.
ESTHER : Ahmad_2020_Drug.Des.Devel.Ther_14_2165
PubMedSearch : Ahmad_2020_Drug.Des.Devel.Ther_14_2165
PubMedID: 32606589

Title : Norditerpenoid alkaloids of Delphinium denudatum as cholinesterase inhibitors - Ahmad_2018_Bioorg.Chem_78_427
Author(s) : Ahmad H , Ahmad S , Ali M , Latif A , Shah SAA , Naz H , Ur Rahman N , Shaheen F , Wadood A , Khan HU , Ahmad M
Ref : Bioorg Chem , 78 :427 , 2018
Abstract : Three new norditerpenoids alkaloids, 1beta-hydroxy,14beta-acetyl condelphine (1), jadwarine-A (2), jadwarine-B (3) along with two known alkaloids isotalatizidine hydrate (4) and dihydropentagynine (5) were isolated from medicinal plant Delphinium denudatum. The structures of natural products 1-5 were established on the basis of HR-EIMS, (1)H and (13)C NMR (1D & 2D) spectroscopic data as well as by comparison from literature data. The structures of compound 1 and 4 were also confirmed by single crystal X-ray diffraction studies. In-vitro AChE and BChE enzyme inhibitory activities of compounds 1-5 and molecular docking studies were performed to investigate the possible molecular inhibitory mechanism of the isolated natural products. Compound 2, 4 and 5 showed competitive inhibitory effects by inhibiting AChE and BChE, respectively, while 1 and 3 showed non-competitive inhibition. This work is the first report that provides a supporting evidence about the use of constituents of Delphinium denudatum in cerebral dementia and Alzheimer diseases.
ESTHER : Ahmad_2018_Bioorg.Chem_78_427
PubMedSearch : Ahmad_2018_Bioorg.Chem_78_427
PubMedID: 29698893

Title : Anti-Alzheimer's Studies on beta-Sitosterol Isolated from Polygonum hydropiper L - Ayaz_2017_Front.Pharmacol_8_697
Author(s) : Ayaz M , Junaid M , Ullah F , Subhan F , Sadiq A , Ali G , Ovais M , Shahid M , Ahmad A , Wadood A , El-Shazly M , Ahmad N , Ahmad S
Ref : Front Pharmacol , 8 :697 , 2017
Abstract : The family Polygonaceae is known for its traditional use in the management of various neurological disorders including Alzheimer's disease (AD). In search of new anti-AD drugs, beta-sitosterol isolated from Polygonum hydropiper was subjected to in vitro, in vivo, behavioral and molecular docking studies to confirm its possibility as a potential anti-Alzheimer's agent. The in vitro AChE, BChE inhibitory potentials of beta-sitosterol were investigated following Ellman's assay. The antioxidant activity was tested using DPPH, ABTS and H2O2 assays. Behavioral studies were performed on a sub-strain of transgenic mice using shallow water maze (SWM), Y-maze and balance beam tests. beta-sitosterol was tested for in vivo inhibitory potentials against cholinesterase's and free radicals in the frontal cortex (FC) and hippocampus (HC). The molecular docking study was performed to predict the binding mode of beta-sitosterol in the active sites of AChE and BChE as inhibitor. Considerable in vitro and in vivo cholinesterase inhibitory effects were observed in the beta-sitosterol treated groups. beta-sitosterol exhibited an IC50 value of 55 and 50 mug/ml against AChE and BChE respectively. Whereas, the activity of these enzymes were significantly low in FC and HC homogenates of transgenic animals. Molecular docking studies also support the binding of beta-sitosterol with the target enzyme and further support the in vitro and in vivo results. In the antioxidant assays, the IC50 values were observed as 140, 120, and 280 mug/ml in the DPPH, ABTS and H2O2 assays respectively. The free radicals load in the brain tissues was significantly declined in the beta-sitosterol treated animals as compared to the transgenic-saline treated groups. In the memory assessment and coordination tasks including SWM, Y-maze and balance beam tests, beta-sitosterol treated transgenic animals showed gradual improvement in working memory, spontaneous alternation behavior and motor coordination. These results conclude that beta-sitosterol is a potential compound for the management of memory deficit disorders like AD.
ESTHER : Ayaz_2017_Front.Pharmacol_8_697
PubMedSearch : Ayaz_2017_Front.Pharmacol_8_697
PubMedID: 29056913

Title : Synthesis and in vitro acetylcholinesterase and butyrylcholinesterase inhibitory potential of hydrazide based Schiff bases - Rahim_2016_Bioorg.Chem_68_30
Author(s) : Rahim F , Ullah H , Taha M , Wadood A , Javed MT , Rehman W , Nawaz M , Ashraf M , Ali M , Sajid M , Ali F , Khan MN , Khan KM
Ref : Bioorg Chem , 68 :30 , 2016
Abstract : To discover multifunctional agents for the treatment of Alzheimer's disease, a series of hydrazide based Schiff bases were designed and synthesized based on multitarget-directed strategy. We have synthesized twenty-eight analogs of hydrazide based Schiff bases, characterized by various spectroscopic techniques and evaluated in vitro for acetylcholinesterase and butyrylcholinesterase inhibition. All compounds showed varied degree of acetylcholinesterase and butyrylcholinesterase inhibition when compared with standard Eserine. Among the series, compounds 10, 3 and 24 having IC50 values 4.12+/-0.01, 8.12+/-0.01 and 8.41+/-0.06muM respectively showed potent acetylcholinesterase inhibition when compared with Eserine (IC50=0.85+/-0.0001muM). Three compounds 13, 24 and 3 having IC50 values 6.51+/-0.01, 9.22+/-0.07 and 37.82+/-0.14muM respectively showed potent butyrylcholinesterase inhibition by comparing with eserine (IC50=0.04+/-0.0001muM). The remaining compounds also exhibited moderate to weak inhibitory potential. Structure activity relationship has been established. Through molecular docking studies the binding interaction was confirmed.
ESTHER : Rahim_2016_Bioorg.Chem_68_30
PubMedSearch : Rahim_2016_Bioorg.Chem_68_30
PubMedID: 27441832

Title : Synthesis of potent urease inhibitors based on disulfide scaffold and their molecular docking studies - Taha_2015_Bioorg.Med.Chem_23_7211
Author(s) : Taha M , Ismail NH , Imran S , Wadood A , Rahim F , Riaz M
Ref : Bioorganic & Medicinal Chemistry , 23 :7211 , 2015
Abstract : Disulfide analogs (1-20) have been synthesized, characterized by HR-MS, (1)H NMR and (13)C NMR and screened for urease inhibitory potential. All compounds were found to have varied degree of urease inhibitory potential ranging in between 0.4+/-0.01 and 18.60+/-1.24muM when compared with standard inhibitor thiourea with IC50 19.46+/-1.20muM. Structure activity relationship has been established. The binding interactions of compounds with enzyme were confirmed through molecular docking. All the synthesized compounds 1-20 are new. Our compounds are cheaply synthesizable with high yield and can further be studied to discovery lead compounds. We further, tested for carbonic anhydrase, PDE1 and butyrylcholinesterase but they show no activity. On the other hand we evaluated all compounds for cytotoxicity they showed no toxicity.
ESTHER : Taha_2015_Bioorg.Med.Chem_23_7211
PubMedSearch : Taha_2015_Bioorg.Med.Chem_23_7211
PubMedID: 26507431

Title : Synthesis, molecular docking, acetylcholinesterase and butyrylcholinesterase inhibitory potential of thiazole analogs as new inhibitors for Alzheimer disease - Rahim_2015_Bioorg.Chem_62_106
Author(s) : Rahim F , Javed MT , Ullah H , Wadood A , Taha M , Ashraf M , Qurat Ul A , Khan MA , Khan F , Mirza S , Khan KM
Ref : Bioorg Chem , 62 :106 , 2015
Abstract : A series of thirty (30) thiazole analogs were prepared, characterized by 1H NMR, 13C NMR and EI-MS and evaluated for Acetylcholinesterase and butyrylcholinesterase inhibitory potential. All analogs exhibited varied butyrylcholinesterase inhibitory activity with IC50 value ranging between 1.59+/-0.01 and 389.25+/-1.75muM when compared with the standard eserine (IC50, 0.85+/-0.0001muM). Analogs 15, 7, 12, 9, 14, 1, 30 with IC50 values 1.59+/-0.01, 1.77+/-0.01, 6.21+/-0.01, 7.56+/-0.01, 8.46+/-0.01, 14.81+/-0.32 and 16.54+/-0.21muM respectively showed excellent inhibitory potential. Seven analogs 15, 20, 19, 24, 28, 30 and 25 exhibited good acetylcholinesterase inhibitory potential with IC50 values 21.3+/-0.50, 35.3+/-0.64, 36.6+/-0.70, 44.81+/-0.81, 46.36+/-0.84, 48.2+/-0.06 and 48.72+/-0.91muM respectively. All other analogs also exhibited well to moderate enzyme inhibition. The binding mode of these compounds was confirmed through molecular docking.
ESTHER : Rahim_2015_Bioorg.Chem_62_106
PubMedSearch : Rahim_2015_Bioorg.Chem_62_106
PubMedID: 26318401