P
Princy Vijayababu
Researcher at Bharathiar University
Publications - 8
Citations - 46
Princy Vijayababu is an academic researcher from Bharathiar University. The author has contributed to research in topics: Salmonella typhi & Quorum sensing. The author has an hindex of 5, co-authored 8 publications receiving 37 citations.
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Journal ArticleDOI
Patulin interference with ATP binding cassette transferring auto inducer −2 in Salmonella typhi and biofilm inhibition via quorum sensing
Princy Vijayababu,Gopinath Samykannu,Jebastin Thomas,Christian Bharathi Antonyraj,Sundara Baalaji Narayanan,Shanmughavel Piramanayagam +5 more
TL;DR: Results will suggest that patulin is the efficient Quorum Sensing Inhibitor to control biofilm formation in S.typhi.
Journal ArticleDOI
Investigations of binding mode insight in Salmonella typhi type-III secretion system tip protein (SipD): A molecular docking and MD simulation study
Gopinath Samykannu,Princy Vijayababu,Christian Bharathi Antonyraj,Sundarabaalaji Narayanan,Syed Ibrahim Basheer Ahamed +4 more
TL;DR: The simulation results showed that Caminoside A binding was highly stable with SipD and Asn318 interaction was more significant for the protein-ligand complex stability, which will provide new knowledge for the development of novel therapeutic strategies against Salmonella typhi.
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In Silico Characterization of B Cell and T Cell Epitopes for Subunit Vaccine Design of Salmonella typhi PgtE: A Molecular Dynamics Simulation Approach.
Gopinath Samykannu,Princy Vijayababu,Christian Bharathi Antonyraj,Perumal Perumal,Sundarabaalaji Narayanan,Syed Ibrahim Basheer Ahamed,Jeyakumar Natarajan +6 more
TL;DR: Computational analysis, molecular docking, and molecular dynamics simulation of PgtE-epitope complex were used to elucidate the binding mode, and the dynamical changes of epitopes were more suitable for vaccine development against typhoid.
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Substrate specificities in Salmonella typhi outer membrane protease (PgtE) from Omptin family – An in silico proteomic approach
TL;DR: The multiple pathogen sequence alignment of Omptin proteases family shows that, interacting residues were conserved among the Omptins and will provide new knowledge for the development of novel therapeutic strategies against S. typhi PgtE and Omptin family proteases.