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Fulltext Prevalence of post-vaccine side effects among COVID-19 immunized community of Southern Pakistan

Qureshi A, Syed Sulaiman SA, Rehman W, Mehmood A, Idrees S, Kumar N

PLoS One, 2023;18(5):e0285736.
PMID: 37220099 DOI: 10.1371/journal.pone.0285736

BACKGROUND: The response to the vaccine may vary among individuals. Hence, it is important to know how often individuals experience side effects after immunization against COVID-19.
OBJECTIVE: This study aimed to assess the incidence of side effects following COVID-19 vaccination across different vaccine recipients in Southern Pakistan and identify the potential factors associated with these side effects in the population.
METHODS: The survey was conducted across Pakistan through Google-forms Links from August to October 2021. The questionnaire included demographic information and COVID-19 vaccine information. Chi-square (x2) was performed for comparative analysis to check the significance level with P <0.05. The final analysis included 507 participants who had received COVID-19 vaccines.
RESULTS: Of the total 507 COVID-19 vaccines recipients, 24.9% received CoronaVac, 36.5% received BBIBP-CorV, 14.2% received BNT162b2, 13.8% received AZD1222, and 10.7% received mRNA-1273. The most prominent side effects after the first dose were fever, weakness, lethargy, and pain at the site of injection. Moreover, the most commonly reported side effects after the second dose were pain at the injection site, headache, body ache, lethargy, fever, chills, flu-like symptoms, and diarrhea.
CONCLUSION: Our results suggested that the side effects due to COVID-19 vaccination can vary between the first and second doses and type of COVID-19 vaccine. Our findings suggest continuing monitoring of vaccine safety and the importance of individualized risk-benefit assessment for COVID-19 immunization.
Synthesis and structure-activity relationship of thiobarbituric acid derivatives as potent inhibitors of urease

Khan KM, Rahim F, Khan A, Shabeer M, Hussain S, Rehman W, et al.

Bioorg Med Chem, 2014 Aug 1;22(15):4119-23.
PMID: 24986232 DOI: 10.1016/j.bmc.2014.05.057

A series of thiobarbituric acid derivatives 1-27 were synthesized and evaluated for their urease inhibitory potential. Exciting results were obtained from the screening of these compounds 1-27. Compounds 5, 7, 8, 11, 16, 17, 22, 23 and 24 showed excellent urease inhibition with IC50 values 18.1 ± 0.52, 16.0 ± 0.45, 16.0 ± 0.22, 14.3 ± 0.27, 6.7 ± 0.27, 10.6 ± 0.17, 19.2 ± 0.29, 18.2 ± 0.76 and 1.61 ± 0.18 μM, respectively, much better than the standard urease inhibitor thiourea (IC₅₀=21 ± 0.11 μM). Compound 3, 4, 10, and 26 exhibited comparable activities to the standard with IC₅₀ values 21.4 ± 1.04 and 21.5 ± 0.61 μM, 22.8 ± 0.32, 25.2 ± 0.63, respectively. However the remaining compounds also showed prominent inhibitory potential The structure-activity relationship was established for these compounds. This study identified a novel class of urease inhibitors. The structures of all compounds were confirmed through spectroscopic techniques such as EI-MS and (1)H NMR.
Isatin based Schiff bases as inhibitors of α-glucosidase: Synthesis, characterization, in vitro evaluation and molecular docking studies

Rahim F, Malik F, Ullah H, Wadood A, Khan F, Javid MT, et al.

Bioorg Chem, 2015 Jun;60:42-8.
PMID: 25955493 DOI: 10.1016/j.bioorg.2015.03.005

Isatin base Schiff bases (1-20) were synthesized, characterized by (1)H NMR and EI/MS and evaluated for α-glucosidase inhibitory potential. Out of these twenty (20) compounds only six analogs showed potent α-glucosidase inhibitory potential with IC50 value ranging in between 2.2±0.25 and 83.5±1.0μM when compared with the standard acarbose (IC50=840±1.73μM). Among the series compound 2 having IC50 value (18.3±0.56μM), 9 (83.5±1.0μM), 11 (3.3±0.25μM), 12 (2.2±0.25μM), 14 (11.8±0.15μM), and 20 (3.0±0.15μM) showed excellent inhibitory potential many fold better than the standard acarbose. The binding interactions of these active analogs were confirmed through molecular docking.
Triazinoindole analogs as potent inhibitors of α-glucosidase: synthesis, biological evaluation and molecular docking studies

Rahim F, Ullah K, Ullah H, Wadood A, Taha M, Ur Rehman A, et al.

Bioorg Chem, 2015 Feb;58:81-7.
PMID: 25528720 DOI: 10.1016/j.bioorg.2014.12.001

A new series of triazinoindole analogs 1-11 were synthesized, characterized by EI-MS and (1)H NMR, evaluated for α-glucosidase inhibitory potential. All eleven (11) analogs showed different range of α-glucosidase inhibitory potential with IC50 value ranging between 2.46±0.008 and 312.79±0.06 μM when compared with the standard acarbose (IC50, 38.25±0.12 μM). Among the series, compounds 1, 3, 4, 5, 7, 8, and 11 showed excellent inhibitory potential with IC50 values 2.46±0.008, 37.78±0.05, 28.91±0.0, 38.12±0.04, 37.43±0.03, 36.89±0.06 and 37.11±0.05 μM respectively. All other compounds also showed good enzyme inhibition. The binding modes of these analogs were confirmed through molecular docking.
Synthesis and molecular docking studies of potent α-glucosidase inhibitors based on biscoumarin skeleton

Khan KM, Rahim F, Wadood A, Kosar N, Taha M, Lalani S, et al.

Eur J Med Chem, 2014 Jun 23;81:245-52.
PMID: 24844449 DOI: 10.1016/j.ejmech.2014.05.010

In our effort directed toward the discovery of new anti-diabetic agent for the treatment of diabetes, a library of biscoumarin derivative 1-18 was synthesized and evaluated for α-glucosidase inhibitory potential. All eighteen (18) compounds displayed assorted α-glucosidase activity with IC50 values 16.5-385.9 μM, if compared with the standard acarbose (IC50 = 906 ± 6.387 μM). In addition, molecular docking studies were carried out to explore the binding interactions of biscoumarin derivatives with the enzyme. This study has identified a new class of potent α-glucosidase inhibitors.
Synthesis of 4-thiazolidinone analogs as potent in vitro anti-urease agents

Rahim F, Zaman K, Ullah H, Taha M, Wadood A, Javed MT, et al.

Bioorg Chem, 2015 Dec;63:123-31.
PMID: 26520885 DOI: 10.1016/j.bioorg.2015.10.005

4-Thiazolidinone analogs 1-20 were synthesized, characterized by (1)H NMR and EI-MS and investigated for urease inhibitory activity. All twenty (20) analogs exhibited varied degree of urease inhibitory potential with IC50 values 1.73-69.65μM, if compared with standard thiourea having IC50 value of 21.25±0.15μM. Among the series, eight derivatives 3, 6, 8, 10, 15, 17, 19, and 20 showed outstanding urease inhibitory potential with IC50 values of 9.34±0.02, 14.62±0.03, 8.43±0.01, 7.3±0.04, 2.31±0.002, 5.75±0.003, 8.81±0.005, and 1.73±0.001μM, respectively, which is better than the standard thiourea. The remaining analogs showed good to excellent urease inhibition. The binding interactions of these compounds were confirmed through molecular docking studies.
Synthesis, in vitro evaluation and molecular docking studies of thiazole derivatives as new inhibitors of α-glucosidase

Rahim F, Ullah H, Javid MT, Wadood A, Taha M, Ashraf M, et al.

Bioorg Chem, 2015 Oct;62:15-21.
PMID: 26162519 DOI: 10.1016/j.bioorg.2015.06.006

A series of thiazole derivatives 1-21 were prepared, characterized by EI-MS and (1)H NMR and evaluated for α-glucosidase inhibitory potential. All twenty one derivatives showed good α-glucosidase inhibitory activity with IC50 value ranging between 18.23±0.03 and 424.41±0.94μM when compared with the standard acarbose (IC50, 38.25±0.12μM). Compound (8) (IC50, 18.23±0.03μM) and compound (7) (IC50=36.75±0.05μM) exhibited outstanding inhibitory potential much better than the standard acarbose (IC50, 38.25±0.12μM). All other analogs also showed good to moderate enzyme inhibition. Molecular docking studies were carried out in order to find the binding affinity of thiazole derivatives with enzyme. Studies showed these thiazole analogs as a new class of α-glucosidase inhibitors.
Synthesis and in vitro acetylcholinesterase and butyrylcholinesterase inhibitory potential of hydrazide based Schiff bases

Rahim F, Ullah H, Taha M, Wadood A, Javed MT, Rehman W, et al.

Bioorg Chem, 2016 10;68:30-40.
PMID: 27441832 DOI: 10.1016/j.bioorg.2016.07.005

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±0.06μM respectively showed potent acetylcholinesterase inhibition when compared with Eserine (IC50=0.85±0.0001μM). Three compounds 13, 24 and 3 having IC50 values 6.51±0.01, 9.22±0.07 and 37.82±0.14μM respectively showed potent butyrylcholinesterase inhibition by comparing with eserine (IC50=0.04±0.0001μM). 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.
Synthesis, in vitro alpha-glucosidase inhibitory potential of benzimidazole bearing bis-Schiff bases and their molecular docking study

Rahim F, Zaman K, Taha M, Ullah H, Ghufran M, Wadood A, et al.

Bioorg Chem, 2020 01;94:103394.
PMID: 31699396 DOI: 10.1016/j.bioorg.2019.103394

Voglibose and acarbose are distinguished α-glucosidase inhibitors used for controlling of diabetes mellitus. Unfortunately, these distinguished and clinically used inhibitors have also numerous side effects. Subsequently, there is still needed to develop safer therapy. Despite of a broad spectrum of biological importance of benzimidazole, it is occasionally evaluated for α-glucosidase activity. Current study deals with the synthesis and biological screening of benzimidazole bearing bis-Schiff bases (1-19) for their α-glucosidase inhibitory activity. All analogues exhibited excellent to good inhibitory potential (IC50 = 2.20 ± 0.1to 88.60 ± 1.70 µM) when compared with standard drug acarbose (IC50 = 38.45 ± 0.80 µM). A structure activity relationship has been established on the basis of electronic effects and position of different substituents present on phenyl ring. In order to rationalize the binding interactions of most active analogues with the active site of α-glucosidase enzyme, molecular docking study was conducted.
New biologically dynamic hybrid pharmacophore triazinoindole-based-thiadiazole as potent α-glucosidase inhibitors: In vitro and in silico study

Khan AA, Rahim F, Taha M, Rehman W, Iqbal N, Wadood A, et al.

Int J Biol Macromol, 2022 Feb 28;199:77-85.
PMID: 34968547 DOI: 10.1016/j.ijbiomac.2021.12.147

Triazinoindole bearing thiadiazole derivatives (1-25) have been synthesized and characterized through different spectroscopic techniques such as 1H, 13C-NMR and HREI-MS. The purpose of the study was to investigate the anti-diabetic activity of the synthesized triazinoindole bearing thiadiazole derivatives by inhibition of α-glucosidase. All synthesized analogues showed outstanding inhibition of α-glucosidase enzyme with IC50 values ranging from 2.5 ± 0.10 to 38.10 ± 0.10 µM as compared to the standard drug acarbose (IC50 = 38.45 ± 0.80 µM). Analogue 4 (IC50 = 2.5 ± 0.10 µM) was identifies as the most potent analogue in the series with fifteen folds more active than standard acarbose. Structure activity relationship (SAR) studies suggested that α-glucosidase activities of triazinoindole bearing thiadiazole are primarily dependent upon on number and position of different substitutions present on phenyl parts. Molecular docking study were conducted of the optimized compounds (i.e., compound 4, 6, and 3 etc. using MOE default parameters), the results revealed that compound 4, 6, and 3 showed numerous key interactions with the target protein, which indicate the high potential of these compounds against the target compound. All these compounds were screened for cytotoxic activity against normal normal Vero cell line and found non-toxic.
Fulltext Multipotent Cholinesterase Inhibitors for the Treatment of Alzheimer's Disease: Synthesis, Biological Analysis and Molecular Docking Study of Benzimidazole-Based Thiazole Derivatives

Hussain R, Ullah H, Rahim F, Sarfraz M, Taha M, Iqbal R, et al.

Molecules, 2022 Sep 18;27(18).
PMID: 36144820 DOI: 10.3390/molecules27186087

Twenty-four analogues of benzimidazole-based thiazoles (1-24) were synthesized and assessed for their in vitro acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitory potential. All analogues were found to exhibit good inhibitory potential against cholinesterase enzymes, having IC50 values in the ranges of 0.10 ± 0.05 to 11.10 ± 0.30 µM (for AChE) and 0.20 ± 0.050 µM to 14.20 ± 0.10 µM (for BuChE) as compared to the standard drug Donepezil (IC50 = 2.16 ± 0.12 and 4.5 ± 0.11 µM, respectively). Among the series, analogues 16 and 21 were found to be the most potent inhibitors of AChE and BuChE enzymes. The number (s), types, electron-donating or -withdrawing effects and position of the substituent(s) on the both phenyl rings B & C were the primary determinants of the structure-activity relationship (SAR). In order to understand how the most active derivatives interact with the amino acids in the active site of the enzyme, molecular docking studies were conducted. The results obtained supported the experimental data. Additionally, the structures of all newly synthesized compounds were elucidated by using several spectroscopic methods like 13C-NMR, 1H-NMR and HR EIMS.