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Self-assembly of robust gold nanoparticle monolayer architectures for quantitative protein interaction analysis by LSPR spectroscopy

Flesch, Julia ; Kappen, Marie ; Drees, Christoph ; You, Changjiang ; Piehler, Jacob

Analytical and bioanalytical chemistry, 2020-05, Vol.412 (14), p.3413-3422 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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Título:
Self-assembly of robust gold nanoparticle monolayer architectures for quantitative protein interaction analysis by LSPR spectroscopy
Autor: Flesch, Julia ; Kappen, Marie ; Drees, Christoph ; You, Changjiang ; Piehler, Jacob
Assuntos: Advances in Direct Optical Detection ; Analytical Chemistry ; Animals ; Biochemistry ; Biocompatibility ; Characterization and Evaluation of Materials ; Chemistry ; Chemistry and Materials Science ; Coatings ; Cytokines ; Ethylene glycol ; Food Science ; Glass substrates ; Gold ; Gold - chemistry ; Histidine ; Humans ; Immobilization ; Immobilized Proteins - metabolism ; Interferon-alpha - metabolism ; Laboratory Medicine ; Lysine ; Metal Nanoparticles - chemistry ; Models, Molecular ; Monitoring/Environmental Analysis ; Monolayers ; Nanoparticles ; Nitrilotriacetic acid ; Poly-L-lysine ; Polyethylene glycol ; Protein Binding ; Protein Interaction Mapping - methods ; Proteins ; Receptor, Interferon alpha-beta - metabolism ; Refractometry - methods ; Research Paper ; Robustness ; Self-assembly ; Spectroscopy ; Spectrum analysis ; Stability analysis ; Substrates ; Surface plasmon resonance ; Surface Plasmon Resonance - methods
É parte de: Analytical and bioanalytical chemistry, 2020-05, Vol.412 (14), p.3413-3422
Notas: Published in the topical collection Advances in Direct Optical Detection with guest editors Antje J. Baeumner, Günter Gauglitz, and Jiri Homola.
Descrição: Localized surface plasmon resonance (LSPR) detection offers highly sensitive label-free detection of biomolecular interactions. Simple and robust surface architectures compatible with real-time detection in a flow-through system are required for broad application in quantitative interaction analysis. Here, we established self-assembly of a functionalized gold nanoparticle (AuNP) monolayer on a glass substrate for stable, yet reversible immobilization of Histidine-tagged proteins. To this end, one-step coating of glass substrates with poly- L -lysine graft poly(ethylene glycol) functionalized with ortho-pyridyl disulfide (PLL-PEG-OPSS) was employed as a reactive, yet biocompatible monolayer to self-assemble AuNP into a LSPR active monolayer. Site-specific, reversible immobilization of His-tagged proteins was accomplished by coating the AuNP monolayer with tris-nitrilotriacetic acid (trisNTA) PEG disulfide. LSPR spectroscopy detection of protein binding on these biocompatible functionalized AuNP monolayers confirms high stability under various harsh analytical conditions. These features were successfully employed to demonstrate unbiased kinetic analysis of cytokine-receptor interactions. Graphical abstract
Editor: Berlin/Heidelberg: Springer Berlin Heidelberg
Idioma: Inglês

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Self-assembly of robust gold nanoparticle monolayer architectures for quantitative protein interaction analysis by LSPR spectroscopy

Flesch, Julia ; Kappen, Marie ; Drees, Christoph ; You, Changjiang ; Piehler, Jacob

Berlin/Heidelberg: Springer Berlin Heidelberg

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