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Article: Inhibitory effect of phytochemicals towards SARS-CoV-2 papain like protease (PLpro) proteolytic and deubiquitinase activity.

Kawall, Anasha / Lewis, Devin S M / Sharma, Avini / Chavada, Krishna / Deshmukh, Rahul / Rayalam, Srujana / Mody, Vicky / Taval, Shashidharamurthy

Frontiers in chemistry

2023 Volume 10, Page(s) 1100460

Abstract: Recent studies have shown that RNA-dependent RNA polymerase (RdRp), 3-chymotrypsin-like protease (3CLpro), and papain-like protease (PLpro) are necessary for SARS-CoV-2 replication. Among these three enzymes, PLpro exhibits both proteolytic and ... ...

Abstract	Recent studies have shown that RNA-dependent RNA polymerase (RdRp), 3-chymotrypsin-like protease (3CLpro), and papain-like protease (PLpro) are necessary for SARS-CoV-2 replication. Among these three enzymes, PLpro exhibits both proteolytic and deubiquitinase (DUB) activity and is responsible for disrupting the host's innate immune response against SARS-CoV-2. Because of this unique property of PLpro, we investigated the inhibitory effects of phytochemicals on the SARS-CoV-2 PLpro enzyme. Our data indicates that the phytochemicals such as catechin, epigallocatechin gallate (EGCG), mangiferin, myricetin, rutin, and theaflavin exhibited inhibitory activity with IC
Language	English
Publishing date	2023-01-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2711776-5
ISSN	2296-2646
ISSN	2296-2646
DOI	10.3389/fchem.2022.1100460
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Dendrimers in medicine

Vicky Mody

Chronicles of Young Scientists, Vol 1, Iss 4, Pp 31-

2010 Volume 32

Keywords	Therapeutics. Pharmacology ; RM1-950 ; Medicine ; R
Language	English
Publishing date	2010-01-01T00:00:00Z
Publisher	Medknow Publications Pvt Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: New therapeutic alternatives to treat Acute Bacterial Skin and Skin Structure Infections (ABSSI)

Vicky V Mody / Ajay Singh

Internet Journal of Medical Update, Vol 10, Iss

2015 Volume 2

Keywords	Medicine ; R ; Medicine (General) ; R5-920
Language	English
Publishing date	2015-07-01T00:00:00Z
Publisher	AKS Publication
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Nanomedicine

Vicky V Mody

Chronicles of Young Scientists, Vol 3, Iss 1, Pp 1-

2012 Volume 2

Keywords	Therapeutics. Pharmacology ; RM1-950 ; Medicine ; R
Language	English
Publishing date	2012-01-01T00:00:00Z
Publisher	Medknow Publications Pvt Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Aloin isoforms (A and B) selectively inhibits proteolytic and deubiquitinating activity of papain like protease (PLpro) of SARS-CoV-2 in vitro.

Lewis, Devin S M / Ho, Joanna / Wills, Savannah / Kawall, Anasha / Sharma, Avini / Chavada, Krishna / Ebert, Maximilian C C J C / Evoli, Stefania / Singh, Ajay / Rayalam, Srujana / Mody, Vicky / Taval, Shashidharamurthy

Scientific reports

2022 Volume 12, Issue 1, Page(s) 2145

Abstract: The most common host entry point of human adapted coronaviruses (CoV) including SARS-CoV-2 is through the initial colonization in the nostril and mouth region which is responsible for spread of the infection. Most recent studies suggest that the ... ...

Abstract	The most common host entry point of human adapted coronaviruses (CoV) including SARS-CoV-2 is through the initial colonization in the nostril and mouth region which is responsible for spread of the infection. Most recent studies suggest that the commercially available oral and nasal rinse products are effective in inhibiting the viral replication. However, the anti-viral mechanism of the active ingredients present in the oral rinses have not been studied. In the present study, we have assessed in vitro enzymatic inhibitory activity of active ingredients in the oral mouth rinse products: aloin A and B, chlorhexidine, eucalyptol, hexetidine, menthol, triclosan, methyl salicylate, sodium fluoride and povidone, against two important proteases of SARS-CoV-2 PLpro and 3CLpro. Our results indicate only aloin A and B effectively inhibited proteolytic activity of PLpro with an IC
MeSH term(s)	Animals ; Binding Sites ; COVID-19/pathology ; COVID-19/virology ; Cell Survival/drug effects ; Chlorocebus aethiops ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/metabolism ; Coronavirus Papain-Like Proteases/antagonists & inhibitors ; Coronavirus Papain-Like Proteases/metabolism ; Emodin/analogs & derivatives ; Emodin/chemistry ; Emodin/metabolism ; Emodin/pharmacology ; Humans ; Molecular Dynamics Simulation ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism ; Protein Isoforms/pharmacology ; SARS-CoV-2/enzymology ; SARS-CoV-2/isolation & purification ; Vero Cells
Chemical Substances	Protein Isoforms ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus Papain-Like Proteases (EC 3.4.22.2) ; papain-like protease, SARS-CoV-2 (EC 3.4.22.2) ; Coronavirus 3C Proteases (EC 3.4.22.28) ; Emodin (KA46RNI6HN) ; alloin (W41H6S09F4)
Language	English
Publishing date	2022-02-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-06104-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Aloin isoforms (A and B) selectively inhibits proteolytic and deubiquitinating activity of papain like protease (PLpro) of SARS-CoV-2 in vitro

Devin S. M. Lewis / Joanna Ho / Savannah Wills / Anasha Kawall / Avini Sharma / Krishna Chavada / Maximilian C. C. J. C. Ebert / Stefania Evoli / Ajay Singh / Srujana Rayalam / Vicky Mody / Shashidharamurthy Taval

Scientific Reports, Vol 12, Iss 1, Pp 1-

2022 Volume 11

Abstract: Abstract The most common host entry point of human adapted coronaviruses (CoV) including SARS-CoV-2 is through the initial colonization in the nostril and mouth region which is responsible for spread of the infection. Most recent studies suggest that the ...

Abstract	Abstract The most common host entry point of human adapted coronaviruses (CoV) including SARS-CoV-2 is through the initial colonization in the nostril and mouth region which is responsible for spread of the infection. Most recent studies suggest that the commercially available oral and nasal rinse products are effective in inhibiting the viral replication. However, the anti-viral mechanism of the active ingredients present in the oral rinses have not been studied. In the present study, we have assessed in vitro enzymatic inhibitory activity of active ingredients in the oral mouth rinse products: aloin A and B, chlorhexidine, eucalyptol, hexetidine, menthol, triclosan, methyl salicylate, sodium fluoride and povidone, against two important proteases of SARS-CoV-2 PLpro and 3CLpro. Our results indicate only aloin A and B effectively inhibited proteolytic activity of PLpro with an IC50 of 13.16 and 16.08 μM. Interestingly, neither of the aloin isoforms inhibited 3CLpro enzymatic activity. Computational structural modelling of aloin A and B interaction with PLpro revealed that, both aloin isoforms form hydrogen bond with Tyr268 of PLpro, which is critical for their proteolytic activity. Furthermore, 100 ns molecular dynamics (MD) simulation studies predicted that both aloin isoforms have strong interaction with Glu167, which is required for PLpro deubiquitination activity. Our results from the in vitro deubiquitinase inhibition assay show that aloin A and B isomers exhibit deubiquitination inhibitory activity with an IC50 value of 15.68 and 17.51 µM, respectively. In conclusion, the isoforms of aloin inhibit both proteolytic and the deubiquitinating activity of SARS-CoV-2 PLpro, suggesting potential in inhibiting the replication of SARS-CoV-2 virus.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2022-02-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Compatibility of Norepinephrine Bitartrate with Levofloxacin and Moxifloxacin During Simulated Y-site Administration.

Mody, Vicky / Shah, Samit / Patel, Jaymin / Thomas, Michael C

International journal of pharmaceutical compounding

2016 Volume 20, Issue 3, Page(s) 236–238

Abstract: The purpose of this study was to determine the physical compatibility and chemical stability of norepinephrine bitartrate with selected fluoroquinolones during simulated intravenous Y-site administration. Simulation of Y-compatibility of intravenous ... ...

Abstract	The purpose of this study was to determine the physical compatibility and chemical stability of norepinephrine bitartrate with selected fluoroquinolones during simulated intravenous Y-site administration. Simulation of Y-compatibility of intravenous fluids can be experimentally demonstrated by mixing equal volumes of two drugs of interest. Hence, we prepared 1:1 mixture of norepinephrine bitartrate and levofloxacin or moxifloxacin by mixing 64 .g/mL of norepinephrine bitartrate individually with clinically relevant concentrations of levofloxacin (5 mg/mL) and moxifloxacin (1.6 mg/mL). The physical stability of these mixtures was assessed via measurement of change in turbidity, and visual inspection for color change, haziness, and precipitate formation. The chemical stability of these mixtures was assessed via high-performance liquid chromatography by evaluating the change in concentration for norepinephrine bitartrate and individual fluoroquinolones, from 0 to 4 hours after mixing. The visual evaluation and turbidity measurements revealed that norepinephrine bitartrate is compatible with individual fluoroquinolones. No color change, haziness, or precipitate formation was observed at 0 and 4 hours when the drugs were mixed at equal volume. The change in turbidity for the mixture as compared to the individual drugs was very minimal (0.001 to 0.004 nephelometric turbidity unit). No significant change in drug concentrations was observed during the 4-hour period for norepinephrine bitartrate and the individual fluoroquinolones following high-performance liquid chromatography analysis of the norepinephrine bitartrate/levofloxacin and norepinephrine bitartrate/moxifloxacin mixtures, which further confirms the stability of this mixture. Our data indicates that norepinephrine bitartrate is compatible with levofloxacin and moxifloxacin, and can be used for intravenous Y-site administration with either of these fluoroquinolone antibiotics.
Language	English
Publishing date	2016-05
Publishing country	United States
Document type	Journal Article
ISSN	1092-4221
ISSN	1092-4221
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Article ; Online: Identification of 3-chymotrypsin like protease (3CLPro) inhibitors as potential anti-SARS-CoV-2 agents.

Mody, Vicky / Ho, Joanna / Wills, Savannah / Mawri, Ahmed / Lawson, Latasha / Ebert, Maximilian C C J C / Fortin, Guillaume M / Rayalam, Srujana / Taval, Shashidharamurthy

Communications biology

2021 Volume 4, Issue 1, Page(s) 93

Abstract: Emerging outbreak of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection is a major threat to public health. The morbidity is increasing due to lack of SARS-CoV-2 specific drugs. Herein, we have identified potential drugs that target ... ...

Abstract	Emerging outbreak of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) infection is a major threat to public health. The morbidity is increasing due to lack of SARS-CoV-2 specific drugs. Herein, we have identified potential drugs that target the 3-chymotrypsin like protease (3CLpro), the main protease that is pivotal for the replication of SARS-CoV-2. Computational molecular modeling was used to screen 3987 FDA approved drugs, and 47 drugs were selected to study their inhibitory effects on SARS-CoV-2 specific 3CLpro enzyme in vitro. Our results indicate that boceprevir, ombitasvir, paritaprevir, tipranavir, ivermectin, and micafungin exhibited inhibitory effect towards 3CLpro enzymatic activity. The 100 ns molecular dynamics simulation studies showed that ivermectin may require homodimeric form of 3CLpro enzyme for its inhibitory activity. In summary, these molecules could be useful to develop highly specific therapeutically viable drugs to inhibit the SARS-CoV-2 replication either alone or in combination with drugs specific for other SARS-CoV-2 viral targets.
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; COVID-19/virology ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/chemistry ; Coronavirus 3C Proteases/metabolism ; Cysteine Proteinase Inhibitors/chemistry ; Cysteine Proteinase Inhibitors/pharmacology ; Drug Discovery ; Humans ; Ligands ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology ; Structure-Activity Relationship ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; Cysteine Proteinase Inhibitors ; Ligands ; Coronavirus 3C Proteases (EC 3.4.22.28)
Language	English
Publishing date	2021-01-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-020-01577-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Identification of 3-chymotrypsin like protease (3CLPro) inhibitors as potential anti-SARS-CoV-2 agents

Vicky Mody / Joanna Ho / Savannah Wills / Ahmed Mawri / Latasha Lawson / Maximilian C. C. J. C. Ebert / Guillaume M. Fortin / Srujana Rayalam / Shashidharamurthy Taval

Communications Biology, Vol 4, Iss 1, Pp 1-

2021 Volume 10

Abstract: Here, the authors identify potential drugs that target 3-chymotrypsin like protease (3CLpro), which is a pivotal protease for the replication of SARS-CoV-2. They found that off-target inhibitors such as ivermectin and micafungin inhibit 3CLpro enzyme ... ...

Abstract	Here, the authors identify potential drugs that target 3-chymotrypsin like protease (3CLpro), which is a pivotal protease for the replication of SARS-CoV-2. They found that off-target inhibitors such as ivermectin and micafungin inhibit 3CLpro enzyme activity, suggesting that these molecules could constitute useful therapies to inhibit SARS-CoV-2 replication.
Keywords	Biology (General) ; QH301-705.5
Language	English
Publishing date	2021-01-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: iOS Appstore-Based Phone Apps for Diabetes Management: Potential for Use in Medication Adherence.

Martinez, Mark / Park, Su Bin / Maison, Isaac / Mody, Vicky / Soh, Lewis Sungkon / Parihar, Harish Singh

JMIR diabetes

2017 Volume 2, Issue 2, Page(s) e12

Abstract: Background: Currently, various phone apps have been developed to assist patients. Many of these apps are developed to assist patients in the self-management of chronic diseases such as diabetes. It is essential to analyze these various apps to ... ...

Abstract	Background: Currently, various phone apps have been developed to assist patients. Many of these apps are developed to assist patients in the self-management of chronic diseases such as diabetes. It is essential to analyze these various apps to understand the key features that would potentially be instrumental in helping patients successfully achieve goals in disease self-management. Objective: The objective of this study was to conduct a review of all the available diabetes-related apps in the iOS App Store to evaluate which diabetic app is more interactive and offers a wide variety of operations such as monitoring glucose, water, carbohydrate intake, weight, body mass index (BMI), medication, blood pressure (BP) levels, reminders or push notifications, food database, charts, exercise management, email, sync between devices, syncing data directly to the prescribers, and other miscellaneous functions such as (Twitter integration, password protection, retina display, barcode scanner, apple watch functionality, and cloud syncing). Methods: Data was gathered using the iOS App Store on an iPad. The search term "diabetes" resulted in 1209 results. Many of the results obtained were remotely related to diabetes and focused mainly on diet, exercise, emergency services, refill reminders, providing general diabetes information, and other nontherapeutic options. We reviewed each app description and only included apps that were meant for tracking blood glucose levels. All data were obtained in one sitting by one person on the same device, as we found that carrying out the search at different times or on different devices (iPhones) resulted in varying results. Apps that did not have a feature for tracking glucose levels were excluded from the study. Results: The search resulted in 1209 results; 85 apps were retained based on the inclusion criteria mentioned above. All the apps were reviewed for average customer ratings, number of reviews, price, and functions. Of all the apps surveyed, 18 apps with the highest number of user ratings were used for in-depth analysis. Of these 18 apps, 50% (9/18) also had a medication adherence function. Our analysis revealed that the Diabetes logbook used by the mySugr app was one of the best; it differentiated itself by introducing fun as a method of increasing adherence. Conclusions: A large variation was seen in patient ratings of app features. Many patient reviewers desired simplicity of app functions. Glucose level tracking and email features potentially helped patients and health care providers manage the disease more efficiently. However, none of the apps could sync data directly to the prescribers. Additional features such as graph customization, availability of data backup, and recording previous entries were also requested by many users. Thus, the use of apps in disease management and patient and health-care provider involvement in future app refinement and development should be encouraged.
Language	English
Publishing date	2017-07-11
Publishing country	Canada
Document type	Journal Article
ISSN	2371-4379
ISSN (online)	2371-4379
DOI	10.2196/diabetes.6468
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