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Research Article
Volume 3, Article ID: 2026.0018
Nisha Suryawanshi
nisha.suryawanshi03@gmail.com
J. Satya Eswari
Satyaeswarij.bt@nitrr.ac.in
Manisha Yadav
manishayadav.nitrr@gmail.com
Sushma Chauhan
sushmac@rpr.amity.edu
Bikash Kumar
bikasmaa@gmail.com
1 Department of Zoology, Govt. College Rau, Indore, India
2 Department of Biotechnology, National Institute of Technology, Raipur, CG, India
3 Amity Institute of Biotechnology, Amity University Chhattisgarh, Raipur, India
* Author to whom correspondence should be addressed
Received: 15 Sep 2025 Accepted: 21 Apr 2026 Available Online: 21 Apr 2026 Published: 02 Jun 2026
Altered glycosylation is a characteristic feature of cancer cells and is closely associated with oncogenesis, malignant differentiation, tumor growth, and metastasis. To test the hypothesis that chitinase may interfere with abnormal glycosylation through interaction with UDP-NAG and DPAGT1, the anticancer potential of chitinase from Thermomyces lanuginosus was evaluated through molecular docking and protein-protein interaction analysis. The chitinase molecule was docked using ligands obtained from the PubChem compound database, and the docking results were analyzed based on docking score, glide score, glide energy, and hydrogen bond interactions. The obtained docking score and glide energy were -5.568 and -53.491, respectively, indicating favorable docking of chitinase with the NAG molecule. In addition, the protein-protein interaction studies showed favorable structure and score models with balanced, electrostatic favored, and hydrophobic favored interactions, suggesting a strong positive interaction between chitinase and DPAGT1. The study concludes that chitinase may be a promising candidate for inhibiting carcinogenesis caused by abnormal glycosylation, either by interacting with UDP-NAG or with DPAGT1, thereby inhibiting the glycosylation process.
Disclaimer: This is not the final version of the article. Changes may occur when the manuscript is published in its final format.