![]() PTGG was conjugated to proteins via a one-pot process molar mass- and grafting density-matched PTGG-lysozyme conjugates were superior to their PEG analogues in terms of enzyme activity and stability against freeze-drying or oxidation the latter is due to sacrificial oxidation of methionine-mimetic PTGG chains. We have here developed an ‘active-stealth’ polymer, poly(thioglycidyl glycerol)(PTGG), which in human plasma is less immunogenic than PEG (35% less complement activation) and features a reactive oxygen species-scavenging and anti-inflammatory action (∼50% less TNF-α in LPS-stimulated macrophages at only 0.1 mg/mL). ![]() First, PEG offers no protection from denaturation during lyophilization, storage, or oxidation (e.g., by biological oxidants, reactive oxygen species) second, PEG’s inherent immunogenicity, leading to hypersensitivity and accelerated blood clearance (ABC), is a growing concern. ![]() PEGylation is by far the most common method employed to overcome immunogenicity and suboptimal pharmacokinetics of, for example, therapeutic proteins but has significant drawbacks. This study addresses well-known shortcomings of poly(ethylene glycol) (PEG)-based conjugates.
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