AI Article Synopsis
- - Tumor lysis syndrome poses a serious risk to humans due to the absence of urate oxidase, prompting research into engineered uricase variants for potential treatment.
- - The study utilized Rosetta software to analyze and design PASylated uricase fusions, aiming to enhance their stability and prolong their half-life by predicting different 3D structures.
- - Findings indicated that the fusion uricase-PAS1-100 showed the highest binding affinity for uric acid, suggesting that PASylation could significantly improve the solubility and stability of urate oxidase for therapeutic applications.
Article Abstract
Tumor lysis syndrome is a life-threatening condition for humans due to the lack of urate oxidase. In this study, several variants of PASylated uricase from the species were analyzed computationally to find the appropriate fusions to solve short half-life and stability concern. The method was performed using Rosetta software to structurally characterize the PAS sequences. The 3D structures of fusions were predicted for fused C- or N-terminally PAS sequences in different length to the uricase. The refinement and energy minimization steps revealed that physicochemical and conformational properties of fusions improved while the structures possessed prolonged PAS sequences. Molecular docking results showed that the highest binding affinity to uric acid belonged to uricase-PAS1-100 by the formation of six hydrogen and four non-hydrogen bonds. Altogether, the results indicated that the PASylation process would be promising upon the production of urate oxidase with improved solubility and stability.
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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7422847 | PMC |
| http://dx.doi.org/10.22088/IJMCM.BUMS.9.1.90 | DOI Listing |
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