ArticleBioconjugate chemistry2017
Tyrosine-Selective Functionalization for Bio-Orthogonal Cross-Linking of Engineered Protein Hydrogels.
Article in Bioconjugate chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Linker-Engineered Tyrosine-Azide Coatings for Stable Strain-Promoted Azide-Alkyne Cycloaddition (SPAAC) Functionalization.Polymers · 2025Article
- Molecular Engineering of Recombinant Protein Hydrogels: Programmable Design and Biomedical Applications.Gels (Basel, Switzerland) · 2025Review
- Advancing Covalent Ligand and Drug Discovery beyond Cysteine.Chemical reviews · 2025Review
- Engineered Protein Hydrogels as Biomimetic Cellular Scaffolds.Advanced materials (Deerfield Beach, Fla.) · 2024Review
- Evolution of Hybrid Hydrogels: Next-Generation Biomaterials for Drug Delivery and Tissue Engineering.Gels (Basel, Switzerland) · 2024Review
- Elastin-like protein hydrogels with controllable stress relaxation rate and stiffness modulate endothelial cell function.Journal of biomedical materials research. Part A · 2023Article
- Silk-Elastin-like Polymers for Acute Intraparenchymal Treatment of the Traumatically Injured Spinal Cord: A First Systematic Experimental Approach.Pharmaceutics · 2022Article
- Novel Strategy for Non-Aqueous Bioconjugation of Substituted Phenyl-1,2,4-triazole-3,5-dione Analogues.Molecules (Basel, Switzerland) · 2022Article
- Chemically Modified Biopolymers for the Formation of Biomedical Hydrogels.Chemical reviews · 2021Review
- Click-functionalized hydrogel design for mechanobiology investigations.Molecular systems design & engineering · 2021Article
- Oxidation-Induced "One-Pot" Click Chemistry.Chemical reviews · 2021Article
- Article
- Electrochemical oxidation induced selective tyrosine bioconjugation for the modification of biomolecules.Chemical science · 2019Article
- Achieving Controlled Biomolecule-Biomaterial Conjugation.Chemical reviews · 2018Review
- Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D.Journal of visualized experiments : JoVE · 2018Article
- Bioorthogonal Strategies for Engineering Extracellular Matrices.Advanced functional materials · 2018Article
- Bioorthogonal Protein Conjugation: Application to the Development of a Highly Sensitive Bioluminescent Immunoassay for the Detection of Interferon-γ.Bioconjugate chemistry · 2017Article
- Spontaneous Self-Organized Order Emerging From Intrinsically Disordered Protein Polymers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnologyReview
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2 authors.
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Abstract
Engineered protein hydrogels have shown promise as artificial extracellular matrix materials for the 3D culture of stem cells due to the ability to decouple hydrogel biochemistry and mechanics. The modular design of these proteins allows for incorporation of various bioactive sequences to regulate cellular behavior. However, the chemistry used to cross-link the proteins into hydrogels can limit what bioactive sequences can be incorporated, in order to prevent nonspecific cross-linking within the bioactive region. Bio-orthogonal cross-linking chemistries may allow for the incorporation of any arbitrary bioactive sequence, but site-selective and scalable incorporation of bio-orthogonal reactive groups such as azides that do not rely on commonly used amine-reactive chemistry is often challenging. In response, we have optimized the reaction of an azide-bearing 4-phenyl-1,2,4-triazoline-3,5-dione (PTAD) with engineered elastin-like proteins (ELPs) to selectively azide-functionalize tyrosine residues within the proteins. The PTAD-azide functionalized ELPs cross-link with bicyclononyne (BCN) functionalized ELPs via the strain-promoted azide-alkyne cycloaddition (SPAAC) reaction to form hydrogels. Human mesenchymal stem cells and murine neural progenitor cells encapsulated within these hydrogels remain highly viable and maintain their phenotypes in culture. Tyrosine-specific modification may expand the number of bioactive sequences that can be designed into protein-engineered materials by permitting incorporation of lysine-containing sequences without concern for nonspecific cross-linking.
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