Quartz crystal microbalance with dissipation coupled to on-chip MALDI-ToF mass spectrometry as a tool for characterising proteinaceous conditioning films on functionalised surfaces

Kirschhöfer, Frank; Rieder, Annika; Prechtl, Carolin; Kühl, Boris; Sabljo, Kristina; Wöll, Christof; Obst, U.; Brenner‐Weiß, Gerald

doi:10.1016/j.aca.2013.10.007

Cited by 14 publications

(11 citation statements)

References 36 publications

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“…For protein identification, a peak list of representative calibrated monoisotopic peptide masses was created for each protein by digestion. These experimental masses were compared to database entries, and probability‐based scoring via the MASCOT search engine was performed . A fixed carbamidomethyl modification was enabled in the MASCOT software.…”

Section: Methodsmentioning

confidence: 99%

The Nature of a Hard Protein Corona Forming on Quantum Dots Exposed to Human Blood Serum

Wang

Maffre

et al. 2016

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Biological responses of cells and organisms to nanoparticle exposure crucially depend on the properties of the protein adsorption layer ("protein corona") forming on nanoparticle surfaces and their characterization is a crucial step toward a deep, mechanistic understanding of their build-up. Previously, adsorption of one type of model protein on nanoparticles was systematically studied in situ by using fluorescence correlation spectroscopy. Here, the first such study of interactions is presented between water-solubilized CdSe/ZnS quantum dots (QDs) and a complex biofluid, human blood serum. Despite the large number of proteins in serum, a protein layer of well-defined (average) thickness forming on QD surfaces is observed. Both the thickness and the apparent binding affinity depend on the type of QD surface ligand. Kinetic experiments reveal that the protein corona formed from serum is irreversibly bound, whereas the one formed from human serum albumin was earlier observed to be reversible. By using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry, the most abundant serum proteins contributing to the formation of a hard corona on the QDs are identified.

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Section: Methodsmentioning

confidence: 99%

The Nature of a Hard Protein Corona Forming on Quantum Dots Exposed to Human Blood Serum

Wang

Maffre

et al. 2016

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“…Recently, via coupling of QCM-D with a subsequent MALDI-ToF analysis, it could be demonstrated that the composition of protein-adlayers after applying mixed protein solutions show pronounced time dependencies. 34 In any case, well-defined model surfaces are essential for studies using SPR and QCM-D. Examples are thiolate-based self-assembled monolayers (SAMs) on Au substrates, which allow the investigation of the interaction of proteins with the organic surfaces in a straightforward fashion.…”

Section: Introductionmentioning

confidence: 99%

Interaction of Human Plasma Proteins with Thin Gelatin-Based Hydrogel Films: A QCM-D and ToF-SIMS Study

et al. 2014

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In the fields of surgery and regenerative medicine, it is crucial to understand the interactions of proteins with the biomaterials used as implants. Protein adsorption directly influences cell-material interactions in vivo and, as a result, regulates, for example, cell adhesion on the surface of the implant. Therefore, the development of suitable analytical techniques together with well-defined model systems allowing for the detection, characterization, and quantification of protein adsorbates is essential. In this study, a protocol for the deposition of highly stable, thin gelatin-based films on various substrates has been developed. The hydrogel films were characterized morphologically and chemically. Due to the obtained low thickness of the hydrogel layer, this setup allowed for a quantitative study on the interaction of human proteins (albumin and fibrinogen) with the hydrogel by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D). This technique enables the determination of adsorbant mass and changes in the shear modulus of the hydrogel layer upon adsorption of human proteins. Furthermore, Secondary Ion Mass Spectrometry and principal component analysis was applied to monitor the changed composition of the topmost adsorbate layer. This approach opens interesting perspectives for a sensitive screening of viscoelastic biomaterials that could be used for regenerative medicine.

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“…In addition to SIMS, MALDI has also been used to couple to the Tof mass analyzer for monitoring the adsorption by molecular ions 129 . MALDI matrix was also used in SIMS sample preparation for enhanced sample ionization 130,131 .…”

Section: Sodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis (Smentioning

confidence: 99%

Quantitation of nonspecific protein adsorption at solid–liquid interfaces for single-cell proteomics

Lee

Sun

2018

Can. J. Chem.

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Protein nonspecific adsorption that occurred at the solid–liquid interface has been subjected to intense physical and chemical characterizations due to its crucial role in a wide range of applications, including food and pharmaceutical industries, medical implants, biosensing, and so on. Protein-adsorption caused sample loss has largely hindered the studies of single-cell proteomics; the prevention of such loss requires the understanding of protein–surface adsorption at the proteome level, in which the competitive adsorption of thousands and millions of proteins with vast dynamic range occurs. To this end, we feel the necessity to review current methodologies on their potentials to characterize — more specifically to quantify — the proteome-wide adsorption. We hope this effort can help advancing single-cell proteomics and trace proteomics.

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Quartz crystal microbalance with dissipation coupled to on-chip MALDI-ToF mass spectrometry as a tool for characterising proteinaceous conditioning films on functionalised surfaces

Cited by 14 publications

References 36 publications

The Nature of a Hard Protein Corona Forming on Quantum Dots Exposed to Human Blood Serum

The Nature of a Hard Protein Corona Forming on Quantum Dots Exposed to Human Blood Serum

Interaction of Human Plasma Proteins with Thin Gelatin-Based Hydrogel Films: A QCM-D and ToF-SIMS Study

Quantitation of nonspecific protein adsorption at solid–liquid interfaces for single-cell proteomics

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