Tuning Polymer Composition Leads to Activity-Stability Tradeoff in Enzyme-Polymer Conjugates.


Journal

Biomacromolecules
ISSN: 1526-4602
Titre abrégé: Biomacromolecules
Pays: United States
ID NLM: 100892849

Informations de publication

Date de publication:
11 09 2023
Historique:
medline: 12 9 2023
pubmed: 23 8 2023
entrez: 23 8 2023
Statut: ppublish

Résumé

Protein-polymer conjugation provides an opportune means to adjust the local environment of proteins and enhance protein stability, performance, and solubility. Although much attention has been focused on tuning protein-polymer interactions, the properties of polymer-modified proteins may also be altered by polymer-polymer interactions. Herein, we sought to better understand the influence of polymer-polymer interactions on

Identifiants

pubmed: 37610792
doi: 10.1021/acs.biomac.3c00396
doi:

Substances chimiques

Polymers 0
polyethylene glycol methacrylate 0
Polyethylene Glycols 3WJQ0SDW1A
Lipase EC 3.1.1.3
sulfobetaine 8CVU22OCJW
Methacrylates 0

Types de publication

Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

4033-4041

Auteurs

Evan A Bisirri (EA)

Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States.

Thaiesha A Wright (TA)

Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States.

Daniel K Schwartz (DK)

Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States.

Joel L Kaar (JL)

Department of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States.

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Classifications MeSH