AI Article Synopsis
- Bioconjugation of polymers to proteins can enhance the stability and effectiveness of biologic systems, but the impact of different polymer structures is not fully understood.
- This study focuses on the first bioconjugation of a cyclic polymer, specifically poly(ethylene glycol), to a model protein (T4 lysozyme) to explore its unique properties.
- By comparing the cyclic polymer-protein conjugate with a linear version and using molecular dynamics simulations, the research aims to highlight the potential of cyclic polymers in improving therapeutic applications.
Article Abstract
Bioconjugation of polymers to proteins is a method to impart improved stability and pharmacokinetic properties to biologic systems. However, the precise effects of polymer architecture on the resulting bioconjugates are not well understood. Particularly, cyclic polymers are known to possess unique features such as a decreased hydrodynamic radius when compared to their linear counterparts of the same molecular weight, but have not yet been studied. Here, we report the first bioconjugation of a cyclic polymer, poly(ethylene glycol) (PEG), to a model protein, T4 lysozyme, containing a single engineered cysteine residue (V131C). We compare the stability and activity of this conjugate with those of a linear PEG-T4 lysozyme analogue of similar molecular weight. Furthermore, we used molecular dynamics (MD) simulations to determine the behavior of the polymer-protein conjugates in solution. We introduce cyclic polymer-protein conjugates as potential candidates for the improvement of biologic therapeutics.
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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11191396 | PMC |
| http://dx.doi.org/10.1021/acs.bioconjchem.4c00202 | DOI Listing |
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