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Cited by 2Erythropoietin and Anemia TreatmentComputational Drug Discovery Methodsvaccines and immunoinformatics approaches

The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.

Unveiling novel hyperglycosylated analog of human erythropoietin: A comprehensive computational exploration

Open access
Thahsin, Naima, Khan, Khairul Islam, Sarwar, Abu Nasor Md Rakib, Sakib, Mohammad Nazmus, Rahman, Mohammad Shahedur·2025·Computational and Structural Biotechnology Reports
DOI 10.1016/j.csbr.2024.100029

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Abstract

Introduction: The capability of human erythropoietin (hEPO) to treat anemia by stimulating erythropoiesis, has made it become one of the world’s leading biopharmaceuticals. An effective way to improve the efficiency of recombinant hEPO drugs is increasing glycosylation which can increase its serum half-life and thereby it’s in vivo biological activity. In this context, the objective of the present study was to explore potential glycosylation sites in hEPO to develop new hyperglycosylated analogous drug. Materials and methods: A rational computational strategy was executed to select compatible region of hEPO for inserting N-linked glycosylation consensus motif (N-X-S/T), thus designing a number of analogs. The 3D models of the analogs were constructed by homology modeling and validated by various in silico tools. The probability of glycosylation was checked and hyperglycosylated models of the selected analogs were developed. Molecular docking and molecular dynamics simulation were performed to select the best analog. Results: Among 40 analogs designed in this study, Analog-71.1 showed most promising results. Four possible sites of this analog showed good probability for glycosylation. According to the molecular docking study, the analog obtained high docking score (2313.711) and formed highest number of (25) hydrogen bonds with erythropoietin receptors, which indicated strong and stable interaction with the receptors. Moreover, the steady trajectory of RMSD, R gyr , RMSF and other findings obtained from MD simulation confirmed the structural stability of the analog. Conclusions: Our overall study has selected Analog-71.1 as a potential candidate to develop new analogous drug with enhanced efficiency, which needs further experimental analyses.

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Research works printed but not linked: 1

  1. Bekker H., Berendsen H., Dijkstra E.J., Achterop S., Drunen R. and Van Der Spoel D.: Gromacs: a parallel computer for molecular dynamics simulations – ScienceOpen. Phys Comput 1993; 92.

Metadata

Authors
Thahsin, N., Khan, K. I., Sarwar, A. N. M. R., Sakib, M. N., & Rahman, M. S.
Affiliations
Jahangirnagar University (BD)
ORCID
Rahman, Mohammad Shahedur
Venue
Computational and Structural Biotechnology Reports
Publisher
American Association for the Advancement of Science (AAAS)
Published
2025-01
Volume
2
ISSN
2950-3639 (ISSN-L)
DOI
10.1016/j.csbr.2024.100029
OpenAlex
W4406199917
Cited by
2
References
65
Citations by year
2026: 1 · 2025: 1
FWCI
1.48
Type
journal article
Language
en
Open access
Licence
Locations
  • Computational and Structural Biotechnology Reports (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
Topics
  • Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
  • Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Keywords
human erythropoietin, hyperglycosylation, N-glycosylation sites, erythropoietin analogs, erythropoietin receptor, anemia treatment, serum half-life, protein structure design, homology modeling, molecular docking, molecular dynamics simulation

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