ArticleBiomacromolecules2020
Synthesis of Zwitterionic and Trehalose Polymers with Variable Degradation Rates and Stabilization of Insulin.
Article in Biomacromolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Exploring the Holdase Activity of Supramolecular Chaperones with Amyloid-Forming Peptides and Insulin.Biomacromolecules · 2026Article
- Encapsulated Control: Shaping Insulin Fibrillation through Polymer Confinement.Biomacromolecules · 2026Article
- Trehalose-Bearing Carriers to Target Impaired Autophagy and Protein Aggregation Diseases.Journal of medicinal chemistry · 2023Review
- Poly(trehalose methacrylate) as an Excipient for Insulin Stabilization: Mechanism and Safety.ACS applied materials & interfaces · 2022Article
- Synthesis and Application of Trehalose Materials.JACS Au · 2022Review
- Charged Poly(ACS biomaterials science & engineering · 2021Article
- Effect of Poly(trehalose methacrylate) Molecular Weight and Concentration on the Stability and Viscosity of Insulin.Macromolecular materials and engineering · 2021Article
- Synthetic linear glycopolymers and their biological applications.Journal of carbohydrate chemistry · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Polymers that stabilize biomolecules are important as excipients in protein formulation. Herein, we describe a class of degradable polymers that have tunable degradation rates depending on the polymer backbone and can stabilize proteins to aggregation. Specifically, zwitterion- and trehalose-substituted polycaprolactone, polyvalerolactone, polycarbonate, and polylactide were prepared and characterized with regards to their hydrolytic degradation and ability to stabilize insulin to mechanical agitation during heat. Ring-opening polymerization (ROP) of allyl-substituted monomers was performed by using organocatalysis, resulting in well-defined alkene-substituted polymers with good control over molecular weight and dispersity. The polymers were then modified by using photocatalyzed thiol-ene reactions to install protein-stabilizing carboxybetaine and trehalose side chains. The resulting polymers were water-soluble and exhibited a wide range of half-lives, from 12 h to more than 3 months. The polymers maintained the ability to stabilize the therapeutic protein insulin from activity loss due to aggregation, demonstrating their potential as degradable excipients for protein formulation.
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Registered trials
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