In Silico Design of Tetanus Toxoid-Derived Fusion Peptides as Antiviral Therapeutics
Keywords:
C fragment, computational modelling, docking, EK1 peptide, tetanus toxoid, SARS-CoV-2
Abstract
This study explores the potential of using the C fragment of tetanus toxoid as a scaffold for designing antiviral peptides targeting SARS-CoV-2. The tetanus toxoid C fragment is a well-characterized and non-toxic protein that can be leveraged to create fusion peptides with enhanced antiviral properties. We employed computational modeling techniques to design fusion proteins by linking the EK1 peptide, known for its inhibitory effects on viral fusion, to the C fragment. The resulting fusion peptides were analyzed for structural integrity and binding efficiency using ProSA and MolProbity for quality assessment. Docking simulations were conducted to evaluate the binding affinity of the designed peptides against the SARS-CoV-2 spike protein, revealing favorable interactions. Additionally, we compared the binding profiles of these novel fusion inhibitors with previously studied peptide inhibitors, demonstrating their competitive binding capabilities. The findings suggest that tetanus toxoid-derived fusion peptides represent a promising class of antiviral therapeutics, with the potential to disrupt SARS-CoV-2 entry mechanisms and contribute to future antiviral strategies.
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[13] Lan, Qiaoshuai, Chao Wang, Jie Zhou, Lijue Wang, Fanke Jiao, Yanbo Zhang, Yanxing Cai, Lu Lu, Shuai Xia, and Shibo Jiang, "25-Hydroxycholesterol-Conjugated EK1 Peptide with Potent and Broad-Spectrum Inhibitory Activity against SARS-CoV-2, Its Variants of Concern, and Other Human Coronaviruses," International Journal of Molecular Sciences, vol. 22, no. 21, p. 11869, 2021.
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[19] Chen, Vincent B., W. Bryan Arendall, Jeffrey J. Headd, Daniel A. Keedy, Robert M. Immormino, Gary J. Kapral, Laura W. Murray, Jane S. Richardson, and David C. Richardson"MolProbity: all-atom structure validation for macromolecular crystallography," Acta Crystallographica Section D: Biological Crystallography, vol. 66, no. 1, pp. 12-21, 2010.
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[28] M. Geoffrey, C. Julian and S. P, "The structure of the tetanus toxin reveals pH- mediated domain dynamics," EMBO reports, vol. 18, no. 8, pp. 1306-1317, 2017.
Published
2023-01-09
How to Cite
Mohan Kumar B. S., Sethupathi Raj S, Kumar, Shalini K. S, Narasimha Murthy V. N, & Rudresh Kumar K.J. (2023). In Silico Design of Tetanus Toxoid-Derived Fusion Peptides as Antiviral Therapeutics. Revista Electronica De Veterinaria, 24(1), 150-156. https://doi.org/10.69980/redvet.v24i1.1330
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