Cheminformatics study: Homology modeling and molecular docking simulations study on milk proteins with most drugs used in dairy sector

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Research Paper 08/06/2024
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Cheminformatics study: Homology modeling and molecular docking simulations study on milk proteins with most drugs used in dairy sector

Zabron Janes, Daniel Shadrack, John Kyaruzi, Hulda Swai, Gabriel Shirima
Int. J. Biosci.24( 6), 123-137, June 2024.
Certificate: IJB 2024 [Generate Certificate]

Abstract

The widespread use of drugs in agriculture and husbandry poses a significant risk to human health through direct exposure via dairy products. In this study, the effects of drug interactions on the conformation, binding modes and affinities was investigated by employing in-silico methods, including homology modeling and molecular docking. Bovine milk proteins (PDB ID: ICE2, 3GC1, 7ER3, 4F5S), and drugs (oxytetracycline CID:54675779, enrofloxacin CID:2082, penicillin, CID: 5904 and albendazole CID:71188) were sourced from the RCSB protein data bank and PubChem database, respectively. Since Bovine β-casein crystal structure is experimentally not resolved and, its structure is absent in PDB bank, homology modeling was used to construct a 3D structure.   MODELLER and I-TASSER were used to model the protein with an accuracy of 87.4% and 89.6%, respectively. Molecular docking simulations reveal that enrofloxacin and oxytetracycline, with Bovine lactoperoxidase (3GC1), showed a strong affinity of -8.4 kcal/mol and -8.3 kcal/mol, respectively. This study provides insights into molecular interactions pivotal for understanding milk quality. The implications extend to environmental, human health, and animal welfare, emphasizing the need for informed strategies in the dairy sector and in pharmaceutical industries during drug design and development.

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