<abstract xmlns="http://www.w3.org/1999/xhtml"><sec><h3>Background</h3><p>Complications in periodontitis and other systemic infections related to <italic>Porphyromonas gingivalis</italic> poses a serious impediment in the treatment process. This leads to the search of novel target proteins to develop newer drugs against <italic>P. gingivalis</italic>. Prolyl tripeptidyl peptidase (ptp-A) seem to be a vital protein in <italic>P. gingivalis</italic> virulence and can be a good target for the novel natural bioactive compounds.</p></sec><sec><h3>Objectives</h3><p>To explore the inhibitory potential of <italic>Rosmarinus officinalis</italic> biocompounds against the ptp-A of <italic>P. gingivalis</italic>.</p></sec><sec><h3>Methods</h3><p>Three-dimensional structure of ptp-A was retrieved from the Protein Data Bank with further optimization of both the protein and ligands. In silico inhibitory potential of the selected ligands against ptp-A was done by AutoDock 2.0 and was visualized with Biovia discovery studio visualizing tool with the assessment of the molecular properties of the ligands against ptp-A by molinspiration calculations and drug likeliness.</p></sec><sec><h3>Results</h3><p>High ptp-A inhibitory effect was observed using rosmarinic acid and luteolin with a bonding energy of −9.81 kcal/mol with 10 hydrogen bond interactions and −9.99 kcal/mol with 7 hydrogen bond interactions, respectively. Carnosic acid and <italic>p</italic>-coumaric acid showed a binding energy of −7.14 kcal/mol and −6.34 kcal/mol, respectively, with 5 hydrogen bond interactions. Molinspiration assessments showed <italic>R. officinalis</italic> compounds as the best drug candidates with the topological polar surface area scores &lt;140 Å toward the best oral bioavailability.</p></sec><sec><h3>Conclusion</h3><p>The carnosic acid, rosmarinic acid, <italic>p</italic>-coumaric acid, and luteolin from <italic>R. officinalis</italic> seem to possess a promising inhibitory effect against ptp-A of <italic>Candida albicans</italic> suggesting ptp-A as the best target to combat <italic>P. gingivalis</italic> with further in vivo validation.</p></sec></abstract>

BackgroundComplications in periodontitis and other systemic infections related to Porphyromonas gingivalis poses a serious impediment in the treatment process. This leads to the search of novel target proteins to develop newer drugs against P. gingivalis. Prolyl tripeptidyl peptidase (ptp-A) seem to be a vital protein in P. gingivalis virulence and can be a good target for the novel natural bioactive compounds.ObjectivesTo explore the inhibitory potential of Rosmarinus officinalis biocompounds against the ptp-A of P. gingivalis.MethodsThree-dimensional structure of ptp-A was retrieved from the Protein Data Bank with further optimization of both the protein and ligands. In silico inhibitory potential of the selected ligands against ptp-A was done by AutoDock 2.0 and was visualized with Biovia discovery studio visualizing tool with the assessment of the molecular properties of the ligands against ptp-A by molinspiration calculations and drug likeliness.ResultsHigh ptp-A inhibitory effect was observed using rosmarinic acid and luteolin with a bonding energy of −9.81 kcal/mol with 10 hydrogen bond interactions and −9.99 kcal/mol with 7 hydrogen bond interactions, respectively. Carnosic acid and p-coumaric acid showed a binding energy of −7.14 kcal/mol and −6.34 kcal/mol, respectively, with 5 hydrogen bond interactions. Molinspiration assessments showed R. officinalis compounds as the best drug candidates with the topological polar surface area scores <140 Å toward the best oral bioavailability.ConclusionThe carnosic acid, rosmarinic acid, p-coumaric acid, and luteolin from R. officinalis seem to possess a promising inhibitory effect against ptp-A of Candida albicans suggesting ptp-A as the best target to combat P. gingivalis with further in vivo validation.

Targeting prolyl tripeptidyl peptidase from <italic>Porphyromonas gingivalis</italic> with the bioactive compounds from <italic>Rosmarinus officinalis</italic>

Department of Microbiology, Saveetha Dental College and Hospitals, Saveetha Institute of Medical and Technical Sciences

Dental Research Cell (BRULAC-DRC), Saveetha Dental College and Hospitals, Saveetha Institute of Medical and Technical Sciences

Asian Biomedicine

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Targeting prolyl tripeptidyl peptidase from  with the bioactive compounds from 

BackgroundComplications in periodontitis and other systemic infections related to Porphyromonas gingivalis poses a serious impediment in the treatment process....

Targeting prolyl tripeptidyl peptidase from Porphyromonas gingivalis with the bioactive compounds from Rosmarinus officinalis

Article Category: Technical report

Published Online: Jun 04, 2020

Page range: 197 - 203

DOI: https://doi.org/10.1515/abm-2019-0061

Keywords
luteolin, ptp-A,, rosmarinic acid

© 2019 Ashwin Kumar Ramalingam et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Targeting prolyl tripeptidyl peptidase from Porphyromonas gingivalis with the bioactive compounds from Rosmarinus officinalis

Article Category: Technical report

Published Online: Jun 04, 2020

Page range: 197 - 203

DOI: https://doi.org/10.1515/abm-2019-0061

Keywordsluteolin, ptp-A,, rosmarinic acid

© 2019 Ashwin Kumar Ramalingam et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Keywords
luteolin, ptp-A,, rosmarinic acid