Dr Priyanka Sharma
@mitbio.edu.in
Assistant Professor; School of Bioengineering Research and Science
School of Bioengineering Science and Research MIT-Arts Design Technology, Pune
Scopus Publications
Scholar Citations
Scholar h-index
Scholar i10-index
Scopus Publications
Sheetal Bhat, Arti Sharma, Priyanka Sharma, Kanwaljeet Singh, Maridul Kundan, Mohd Fayaz, Mir Abdul Wajid, Sumeet Gairola, and Prashant Misra
Elsevier BV
Sushila Dahiya, Amit Katiyar, Sumit Rai, Priyanka Sharma, Punit Kaur, and Arti Kapil
Elsevier BV
Priyanka Sharma, Mir Abdul Wajid, Mohd Fayaz, Sheetal Bhat, Abhishek Kumar Nautiyal, Sabha Jeet, Arvind Kumar Yadav, Deepika Singh, Ravi Shankar, Sumeet Gairola,et al.
Springer Science and Business Media LLC
Mohd Fayaz, Maridul Kundan, Umar Gani, Priyanka Sharma, Mir Abdul Wajid, Kajal Katoch, Vikash Babu, Sumeet Gairola, and Prashant Misra
Elsevier BV
P. K. Arora, S. Kumar, S. K. Bansal, and P. C. Sharma
Rasayan Journal of Chemistry
The present study focuses on the synthesis of some 2-methoxyphenylquinazolin-4-one incorporated chalcone hybrids to evaluate their cytotoxic potential by MTT assay, and their affinity to bind with T790M mutated epidermal growth factor receptor (EGFR; protein data bank Id: 5Y9T) and G12D mutated Kirsten rat sarcoma (K-RAS; protein data bank Id:4EPT) by molecular docking (auto dock-4) by employing validated docking parameters. Against the lung cancer cells (A549), except C7 (IC50: 48.22 g/ml), the other title compounds exhibited more cytotoxicity (IC50 16.88g/ml to 33.98g/ml) than the erlotinib (reference). Against the colorectal cancer cells, the compound C4 (IC50: 9.74 g/ml) exhibited more cytotoxicity than the reference (IC50: 16.13 g/ml). For the normal cell lines (Vero), the compound C1 (IC50 27.88g/ml) is less toxic to normal cells, than the reference. The title compounds can be a boon for the development of smart anticancer drugs with dual target virtue
Aarti Bains, Priyanka Sharma, Sukhdeep Kaur, Rahul Yadav, Anil Kumar, Kandi Sridhar, Prince Chawla, and Minaxi Sharma
Elsevier BV
Arun Dev Singh, Kanika Khanna, Jaspreet Kour, Shalini Dhiman, Tamanna Bhardwaj, Kamini Devi, Neerja Sharma, Pardeep Kumar, Nitika Kapoor, Priyanka Sharma,et al.
Elsevier BV
Mohd Salman, Priyanka Sharma, Mukesh Kumar, A S Ethayathulla, and Punit Kaur
Oxford University Press (OUP)
Abstract Antimicrobial resistance in bacteria poses major challenges in selection of the therapeutic regime for managing the infectious disease. There is currently an upsurge in the appearance of multiple drug resistance in bacterial pathogens and a decline in the discovery of novel antibiotics. DNA gyrase is an attractive target used for antibiotic discovery due to its vital role in bacterial DNA replication and segregation in addition to its absence in mammalian organisms. Despite the presence of successful antibiotics targeting this enzyme, there is a need to bypass the resistance against this validated drug target. Hence, drug development in DNA gyrase is a highly active research area. In addition to the conventional binding sites for the novobiocin and fluoroquinolone antibiotics, several novel sites are being exploited for drug discovery. The binding sites for novel bacterial type II topoisomerase inhibitor (NBTI), simocyclinone, YacG, Thiophene and CcdB are structurally and biochemically validated active sites, which inhibit the supercoiling activity of topoisomerases. The novel chemical moieties with varied scaffolds have been identified to target DNA gyrase. Amongst them, the NBTI constitutes the most advanced DNA gyrase inhibitor which are in phase III trial of drug development. The present review aims to classify the novel binding sites other than the conventional novobiocin and quinolone binding pocket to bypass the resistance due to mutations in the DNA gyrase enzyme. These sites can be exploited for the identification of new scaffolds for the development of novel antibacterial compounds.
Reshu Saxena, Priyanka Sharma, Sandeep Kumar, Niteshkumar Agrawal, Sumit Kumar Sharma, and Amit Awasthi
Elsevier BV
Priyanka Sharma, S.M. Shivaraj, Varsha Arun Mahadik, and Narendra Kadoo
CRC Press
Ankita Kumari, Archana Kumari, Himanshu Sharma, Priyanka Sharma, Sayan Bhattacharya, Tulika Mishra, Abdel Rahman Al-Tawaha, Milan Kumar Lal, Rahul Kumar Tiwari, Sayanti Mandal,et al.
Springer Nature Switzerland
Shalini Dhiman, Kanika Khanna, Pardeep Kumar, Tamanna Bhardwaj, Kamini Devi, Neerja Sharma, Priyanka Sharma, Priya Arora, Nitika Kapoor, Anket Sharma,et al.
Springer Science and Business Media LLC
Priyanka Maiti, Mahesha Nand, Shalini Mathpal, Shadma Wahab, Jagdish Chandra Kuniyal, Priyanka Sharma, Tushar Joshi, Muthannan Andavar Ramakrishnan, and Subhash Chandra
Informa UK Limited
The emergence and immune evasion ability of SARS-CoV-2 Omicron strains, mainly BA.5.2 and BF.7 and other variants of concern have raised global apprehensions. With this context, the discovery of multitarget inhibitors may be proven more comprehensive paradigm than its one-drug-to-one target counterpart. In the current study, a library of 271 phytochemicals from 25 medicinal plants from the Indian Himalayan Region has been virtually screened against SARS-CoV-2 by targeting nine virus proteins, viz., papain-like protease, main protease, nsp12, helicase, nsp14, nsp15, nsp16, envelope, and nucleocapsid for screening of a multi-target inhibitor against the viral replication. Initially, 94 phytochemicals were screened by a hybrid machine learning model constructed by combining 6 confirmatory bioassays against SARS-CoV-2 replication using an instance-based learner lazy k-nearest neighbour classifier. Further, 25 screened compounds with excellent drug-like properties were subjected to molecular docking. The phytochemical Cepharadione A from the plant Piper longum showed binding potential against four proteins with the highest binding energy of -10.90 kcal/mol. The compound has acceptable absorption, distribution, metabolism, excretion, and toxicity properties and exhibits stable binding behaviour in terms of root mean square deviation (0.068 ± 0.05 nm), root-mean-square fluctuation, hydrogen bonds, solvent accessible surface area (83.88-161.89 nm2), and molecular mechanics Poisson-Boltzmann surface area during molecular dynamics simulation of 200 ns with selected target proteins. Concerning the utility of natural compounds in the therapeutics formulation, Cepharadione A could be further investigated as a remarkable lead candidate for the development of therapeutic drugs against SARS-CoV-2.Communicated by Ramaswamy H. Sarma.
Tamanna Bhardwaj, Indu Sharma, Dhriti Kapoor, Arun Dev Singh, Shalini Dhiman, Priyanka Sharma, Kamini Devi, Neerja Sharma, Tunisha Verma, Amrit Pal Singh,et al.
CRC Press
Arun Dev Singh, Jaspreet Kour, Pardeep Kumar, Neerja Sharma, Priyanka Sharma, Isha Madaan, Indu Sharma, Nitika Kapoor, Amrit Pal Singh, and Renu Bhardwaj
Elsevier
Shalini Dhiman, Arun Dev Singh, Jaspreet Kour, Tamanna Bhardwaj, Kamini Devi, Raman Tikoria, Puja Ohri, Renu Bhardwaj, and Priyanka Sharma
Elsevier
Priyanka Sharma, Nitika Kapoor, Shalini Dhiman, Jaspreet Kour, Arun Dev Singh, Ashutosh Sharma, and Renu Bhardwaj
Elsevier
Tushar Joshi, Shalini Mathpal, Priyanka Sharma, Satish Chandra Pandey, Priyanka Maiti, Mahesha Nand, and Subhash Chandra
Elsevier
Deepali Gupta, Mukesh Kumar, Priyanka Sharma, Trishala Mohan, Amresh Prakash, Renu Kumari, and Punit Kaur
MDPI AG
The COVID-19 pandemic, caused by SARS-CoV-2, emerges as a global health problem, as the viral genome is evolving rapidly to form several variants. Advancement and progress in the development of effective vaccines and neutralizing monoclonal antibodies are promising to combat viral infections. In the current scenario, several lineages containing “co-mutations” in the receptor-binding domain (RBD) region of the spike (S) protein are imposing new challenges. Co-occurrence of some co-mutations includes delta (L452R/T478K), kappa (L452R/E484Q), and a common mutation in both beta and gamma variants (E484K/N501Y). The effect of co-mutants (L452R/E484Q) on human angiotensin-converting enzyme 2 (hACE2) binding has already been elucidated. Here, for the first time, we investigated the role of these RBD co-mutations (L452R/E484Q) on the binding affinity of mAbs by adopting molecular dynamics (MD) simulation and free-energy binding estimation. The results obtained from our study suggest that the structural and dynamic changes introduced by these co-mutations reduce the binding affinity of the viral S protein to monoclonal antibodies (mAbs). The structural changes imposed by L452R create a charged patch near the interfacial surface that alters the affinity towards mAbs. In E484Q mutation, polar negatively charged E484 helps in the formation of electrostatic interaction, while the neutrally charged Q residue affects the interaction by forming repulsive forces. MD simulations along with molecular mechanics-generalized Born surface area (MMGBSA) studies revealed that the REGN 10933, BD-368-2, and S2M11 complexes have reduced binding affinity towards the double-mutant RBD. This indicates that their mutant (MT) structures have a stronger ability to escape from most antibodies than the wild type (WT). However, EY6A Ab showed higher affinity towards the double MT-RBD complex as compared to the WT. However, no significant effect of the per-residue contribution of double-mutated residues was observed, as this mAb does not interact with the region harboring L452 and E484 residues.
Priyanka Sharma, Sushila Dahiya, Punit Kaur, and Arti Kapil
Elsevier BV
Priyanka Sharma, Geetika Sethi, Manish Kumar Tripathi, Shweta Rana, Harpreet Singh, and Punit Kaur
Springer Nature Singapore
Roshan Gul, Priyanka Sharma, Raman Kumar, Ahmad Umar, Ahmed A. Ibrahim, Mohsen A.M. Alhamami, Vivek Sheel Jaswal, Manish Kumar, Ashutosh Dixit, and Sotirios Baskoutas
Elsevier BV
Ghanshyam Teli, Priyanka Sharma, and Pooja A. Chawla
Informa UK Limited
Abstract A series of 4-thiazolidinone conjugates bearing quinoline/indole/furan scaffolds were designed as potential anti-breast cancer agents, synthesized, and investigated for their anti-breast cancer, and anti-oxidant activity. The anticancer activity was performed using MTT assay against breast cancer cell lines such as MCF-7 and MDA-MB-231 and the results demonstrated that most of the compounds were sensitive to cancer cell lines. Compounds GT1, GT2 and GT5 showed remarkable potency against MCF-7 cell lines with IC50 values of 11.64 µM, 11.27 µM and 11.37 µM respectively in comparison to standard drug doxorubicin with IC50 value of 11.80 µM. Compounds GT2 and GT5 exerted higher cytotoxic activity against the MDA-MD-231 cell line with IC50 value of 17.60 µM and 15.09 µM respectively than doxorubicin (IC50: 18.35 µM). The anti-oxidant activity was also performed by DPPH and hydrogen peroxide scavenging assay. Compounds GT2 and GT7 showed higher free radical scavenging activity with IC50 value of 11.39 µM and 11.28 µM respectively against DPPH assay and 10.99 µM and 11.20 µM respectively against hydrogen peroxide assay. The molecular docking study was carried out against estrogen receptor alpha (PDB ID: 4IVY) to identify the mechanism of action of synthesized compounds using molecular docking and molecular dynamics simulation. The results showed that compounds GT1, GT2, and GT5 showed higher docking score −110.922 kcal/mol, −124.618 kcal/mol and-116.029 kcal/mol respectively as compared to reference (doxorubicin) drug (-109.847 kcal/mol). The ADME and toxicity profile was predicated by Schrodinger QikProp program. All the synthesized compounds showed no violation of Lipinski’s rule except GT2. The molecule insight behavior was predicted by using MD simulation. According to in silico and in vitro studies GT1, GT2, and GT5 showed anti-cancerous activity against MCF-7. Graphical Abstract
Priyanka Sharma, Tanuja Joshi, Tushar Joshi, Shalini Mathpal, Priyanka Maiti, Mahesh Nand, Subhash Chandra, and Sushma Tamta
Informa UK Limited
Abstract A computational investigation was carried out to find out potential phytochemicals that could inhibit the binding of human angiotensin-converting enzyme-2 (ACE2) receptors to spike protein of SARS-CoV-2 which is an essential step to gain entry inside human cells and onset of viral infection known as Coronavirus disease (COVID-19). A library of phytochemicals was screened by virtual screening against ACE2 receptors resulting in twenty phytochemicals out of 686 which had binding energy (−11.8 to −6.9 kcal/mol). Drug-likeness gave five hits, but ADMET analysis yielded 4 nontoxic hit phytochemicals. Molecular dynamics simulation of four-hit compounds resulted in acceptable stability and good dynamics behavior. These phytochemicals are Hinokinin, Gmelanone, Isocolumbin, and Tinocordioside, from Vitis vinifera, Gmelina arborea, and Tinospora cordifolia. The above-mentioned phytochemicals may be promising ACE2 inhibitors and can prevent infection of SARS-CoV-2 by inhibiting the entry of the virus into host cells. Communicated by Ramaswamy H. Sarma