ArticleBiotechnologia2024
Investigation of the new substitution glycine to alanine within the Kringle-2 domain of reteplase: a molecular dynamics study.
Article in Biotechnologia, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Computational Modeling and MM-PBSA-Based Molecular Dynamics Investigation of Unexplored tRNA Isoleucine Lysidine Synthetase from Mycobacterium tuberculosis with Hyperbranched Amoxicilloyl-Poly-L-Lysine.Journal of molecular modeling · 2026Article
- Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
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Authors and funding
6 authors.
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Abstract
Background: Recombinant plasminogen activator (r-PA) consists of the Kringle-2 and protease domains of human tissue-type plasminogen. It is used clinically to treat coronary artery thrombosis and acute myocardial infarction. However, the expression and production of reteplase (r-PA) are limited due to its susceptibility to proteolysis during manufacturing processes. Therefore, efforts have been made to address this limitation. Materials and methods: To enhance the conformational stability of r-PA and increase its resistance to proteolysis, we used Gly 6 Ala substitutions in the Kringle-2 domain through Results: The findings revealed that a single glycine-alanine substitution (G39A) enhanced the conformational stability of r-PA, as evidenced by improvements in RMSD, RMSF, radius of gyration, surface accessibility, hydrogen bond formation, eigenvector projection, and density analysis. Conclusion: The conformational stability of r-PA conferred by glycine replacement with alanine may decrease the propensity for proteolysis in protease - rich environments across various recombinant systems and potentially enhance its production and expression levels.
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