Evidence map›Paper›PMID 41803206›Full record

ArticleScientific reports2026

Streptomyces koyangensis L-asparaginase: computational prediction of dual-mechanism BCL-2 interaction in acute lymphoblastic leukemia.

Gayatri Solanki, Chirag Prajapati, Rekha Gadhvi, Laxmikant Kamble, Mukesh Chandra Sharma, Sunil Tulshiram Hajare

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Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Gayatri SolankiDepartment of Biotechnology, Veer Narmad South Gujarat University, Surat, Gujarat, India.
Chirag PrajapatiDepartment of Biotechnology, Veer Narmad South Gujarat University, Surat, Gujarat, India.
Rekha GadhviParul Institute of Applied Sciences (PIAS), Parul University, Vadodara, Gujarat, India.
Laxmikant KambleSchool of Life Sciences, SRTMU, Nanded, MS, India.
Mukesh Chandra SharmaSchool of Pharmacy, Devi Ahilya Vishwavidhyalaya, Indore, MP, India.
Sunil Tulshiram HajareDepartment of Biotechnology, School of computational and Natural Science, Dilla University, Dilla, Ethiopia. sunilhajare@gmail.com.ORCID http://orcid.org/0000-0002-6118-9471

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present research uses integrative computational analysis to assess Streptomyces koyangensis L-asparaginase as a therapeutic against acute lymphoblastic leukemia (ALL), overcoming immunogenicity and cross-reactivity issues with E. coli and Erwinia carotovora enzymes. We characterized enzyme-oncoprotein interactions using six in silico methods: homology modeling (SWISS-MODEL, AlphaFold2), molecular docking (ClusPro, HADDOCK, AutoDock Vina), 100 ns molecular dynamics (MD) (GROMACS), and pharmacophore modeling (LigandScout). Exceptional stability of the S. koyangensis-BCL-2 complex was revealed: binding energy − 13.8 kcal/mol; RMSD < 2.5 Å; Molecular Mechanics Poisson-Boltzmann Surface Area (MM-PBSA) -68.4 ± 5.2 kcal/mol, forming a 2,145 Ų interface with 80 interacting residues. Pharmacophore modeling identified eight features targeting Asp42, Glu78, and Arg156 for rational engineering. This suggests a potential dual mechanism involving asparagine depletion and predicted BCL-2 binding interactions that may enhance leukemic apoptosis, pending experimental validation. Comparative analysis confirmed S. koyangensis demonstrated statistically significant superior binding affinity compared to alternatives (P < 0.01), offering a computational framework for identifying potential anti-cancer biotherapeutic candidates requiring experimental validation.

Indexed as

AsparaginasePrecursor Cell Lymphoblastic Leukemia-LymphomaProto-Oncogene Proteins c-bcl-2StreptomycesAmino Acid SequenceAntineoplastic AgentsHumansModels, MolecularMolecular Docking SimulationMolecular Dynamics SimulationPharmacophoreProtein BindingAntineoplastic AgentsAsparaginaseProto-Oncogene Proteins c-bcl-2Acute lymphoblastic leukemiaL-asparaginaseMolecular dockingProtein–protein interactionsStreptomyces koyangensis

Identifiers

PMID41803206
PMCPMC13087299

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.