Proceedings of the conference BioSangam 2022: Emerging trends in Biotechnology (BIOSANGAM 2022)

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Docking and Molecular Dynamics Simulation Studies for the Evaluation of Laccase Mediated Biodegradation of Triclosan

Authors
G. Ranimol1, 2, C. B. Devipriya2, Swetha Sunkar1, *
1Department of Bioinformatics, Sathyabama Institute of Science and Technology, (Deemed to be University), Chennai, Tamil Nadu, 600119, India
2Department of Biotechnology, Sahrdaya College of Engineering and Technology, Kodakara, Kerala, 680684, India
*Corresponding author. Email: swetha.biotech@sathyabama.ac.in
Corresponding Author
Swetha Sunkar
Available Online 14 December 2022.
DOI
10.2991/978-94-6463-020-6_20How to use a DOI?
Keywords
Triclosan; laccase; dioxin; stability; docking; simulation
Abstract

Triclosan (TCA) is an antibacterial and antimicrobial compound that is incorporated into toothpaste, soap, and liquid dishwasher. Continuous TCA exposure may contribute to the emergence of antibiotic-resistant bacteria in the microbiome. Triclosan also reacts to form dioxins, which bioaccumulate and are toxic to aquatic organisms, impedes the thyroid hormone metabolism of the human body. Laccases are multi copper-containing enzymes that can degrade the aromatic compounds and thus reduce their toxicity. To effectively degrade the compound, it is essential to understand the molecular function of the enzyme. Hence, a molecular docking study of laccase enzymes with Triclosan was done. The Tramates versicolor laccase structure was retrieved from PDB and ligand structure was taken from Pubchem. The binding mode and interaction of TCA and laccase were studied using Auto dock Vina software and the stability of the docked complex had been explored via Molecular Dynamics (MD) simulation study using Schrodinger Desmonde. The binding affinity score was found to be −6.5kcal/mol. The majority of the residues in RMSF were within the 2.5Å limit. The radius of gyration remained within the range from 21.7 to 22.1Å for Laccase – TCA complex throughout the 50 ns simulation. MD simulation results show that the enzyme complex remains stable all through the catalytic action.

Copyright
© 2023 The Author(s)
Open Access
Open Access This chapter is licensed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

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Volume Title
Proceedings of the conference BioSangam 2022: Emerging trends in Biotechnology (BIOSANGAM 2022)
Series
Advances in Biological Sciences Research
Publication Date
14 December 2022
ISBN
10.2991/978-94-6463-020-6_20
ISSN
2468-5747
DOI
10.2991/978-94-6463-020-6_20How to use a DOI?
Copyright
© 2023 The Author(s)
Open Access
Open Access This chapter is licensed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

Cite this article

risenwbib
TY  - CONF
AU  - G. Ranimol
AU  - C. B. Devipriya
AU  - Swetha Sunkar
PY  - 2022
DA  - 2022/12/14
TI  - Docking and Molecular Dynamics Simulation Studies for the Evaluation of Laccase Mediated Biodegradation of Triclosan
BT  - Proceedings of the conference BioSangam 2022: Emerging trends in Biotechnology (BIOSANGAM 2022)
PB  - Atlantis Press
SP  - 205
EP  - 213
SN  - 2468-5747
UR  - https://doi.org/10.2991/978-94-6463-020-6_20
DO  - 10.2991/978-94-6463-020-6_20
ID  - Ranimol2022
ER  -