Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 11, Issue 40, Pages 36391-36398Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsami.9b12746
Keywords
protein immobilization; bioorthogonal ligation; genetic code expansion; biomaterial; biointerface; tetrazine; sTCO; inverse electron demand Diels-Alder
Funding
- National Science Foundation (NSF) [1518265]
- Oregon State University
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1518265] Funding Source: National Science Foundation
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Biomaterials based on immobilized proteins are key elements of many biomedical and industrial technologies. However, applications are limited by an inability to precisely construct materials of high homogeneity and defined content. We present here a general protein-limited immobilization strategy by combining the rapid, bioorthogonal, and biocompatible properties of a tetrazine-strained trans-cyclooctene reaction with genetic code expansion to site-specifically place the tetrazine into a protein. For the first time, we use this strategy to immobilize defined amounts of oriented proteins onto beads and flat surfaces in under 5 min at submicromolar concentrations without compromising activity. This approach opens the door to generating and studying diverse protein-based biomaterials that are much more precisely defined and characterized, providing a greater ability to engineer properties across a wide range of applications.
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