Proteomic Analysis of Biomaterial Surfaces after Contacting with Body Fluids by MALDI-ToF Mass Spectroscopy
Source abstract
Abstract
We developed a method to identify proteins adsorbed on solid surfaces from a solution containing a complex mixture of proteins by using Matrix-Assisted Laser Desorption/Ionization-Time of Flight mass (MALDI-ToF mass) spectroscopy. In the method, we performed all procedures of peptide mass fingerprint method including denaturation, reduction, alkylation, digestion, and spotting of matrix on substrates. The method enabled us to avoid artifacts of pipetting that could induce changes in the composition. We also developed an algorithm to identify the adsorbed proteins. In this work, we demonstrate the identification of proteins adsorbed on self-assembled monolayers (SAMs). Our results show that the composition of proteins on the SAMs critically depends on the terminal groups of the molecules constituting the SAMs, indicating that the competitive adsorption of protein molecules is largely affected by protein-surface interaction. The method introduced here can provide vital information to clarify the mechanism underlying the responses of cells and tissues to biomaterials.
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Research context
OpenAlex topics: Mass Spectrometry Techniques and Applications · Advanced Proteomics Techniques and Applications · Ion-surface interactions and analysis
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Materials Science and Engineering, School of Materials and Chemical Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa 226-8502, Japan
Surface and Interface Science Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
JST-PRESTO, 4-1-8 Hon-cho, Kawaguchi, Saitama 332-0012, Japan
Funding
Japan Science and Technology Agency
References (45)
Show source-provided references
1. The roles of water molecules at the biointerface of medical polymers10.1038/pj.2012.229 ↗
2. Patterning proteins and cells using soft lithography10.1016/S0142-9612(99)00165-9 ↗
3. An extracellular matrix microarray for probing cellular differentiation10.1038/nmeth736 ↗
4. Role of the extracellular matrix in regulating stem cell fate10.1038/nrm3620 ↗
5. SPR Studies of the Nonspecific Adsorption Kinetics of Human IgG and BSA on Gold Surfaces Modified by Self-Assembled Monolayers (SAMs)10.1006/jcis.1996.4586 ↗
6. Chemisorption of proteins and their thiol derivatives onto gold surfaces: Characterization based on electrochemical nonlinearity10.1016/S0301-4622(96)02208-9 ↗
7. Characterization of Ferritin Adsorption onto Gold10.1006/jcis.1996.4625 ↗
8. Structural changes in hemoglobin during adsorption to solid surfaces: Effects of pH, ionic strength, and ligand binding10.1073/pnas.95.21.12271 ↗
9. Multifrequency evaluation of different immunosorbents on acoustic plate mode sensors10.1021/ac9504777 ↗
10. Adsorptions of plasma proteins and their elutabilities from a polysiloxane surface studied by an on-line acoustic wave sensor10.1021/ac9909094 ↗
11. Sensitivity of the acoustic waveguide biosensor to protein binding as a function of the waveguide properties10.1016/S0956-5663(03)00080-0 ↗
12. Interactions of blood proteins with poly(isobutylcyanoacrylate) nanoparticles decorated with a polysaccharidic brush10.1016/j.biomaterials.2005.01.019 ↗
13. Solution structure and direct imaging of fibronectin adsorption to solid surfaces by scanning force microscopy and cryo-electron microscopy
14. In vitro plasma protein adsorption and kallikrein formation on 3-mercaptopropionic acid, L-cysteine and glutathione immobilized onto gold10.1002/jbm.820280806 ↗
15. Characterization of polyelectrolyte-protein multilayer films by atomic force microscopy, scanning electron microscopy, and Fourier transform infrared reflection-absorption spectroscopy10.1021/la971288h ↗
16. Temperature dependence of the protein resistance of poly- and oligo(ethylene glycol)-terminated alkanethiolate monolayers10.1021/la010576h ↗
17. Quantification of the surface density of a fluorescent label with the optical microscope10.1002/(SICI)1097-4636(200004)50:1<90::AID-JBM13>3.0.CO;2-3 ↗
18. Preparation and microscopic visualization of multicolor luminescent immunophosphors10.1002/cyto.990130603 ↗
19. Rapid identification of proteins by peptide-mass fingerprinting10.1016/0960-9822(93)90195-T ↗
20. Peptide mass fingerprint sequence coverage from differently stained proteins on two-dimensional electrophoresis patterns by matrix assisted laser desorptiodionization-mass spectrometry (MALDI-MS)10.1002/elps.1150190607 ↗
21. Adsorption of plasma proteins on uncoated PLGA nanoparticles10.1016/j.ejpb.2012.11.030 ↗
22. Proteomic analysis of protein adsorption capacity of different haemodialysis membranes10.1039/c2mb05393d ↗
23. Proteomic investigations on the effect of different membrane materials on blood protein adsorption during haemodialysis
24. Adsorption of cationic peptides to solid surfaces of glass and plastic10.1371/journal.pone.0122419 ↗
25. Quartz crystal microbalance with dissipation coupled to on-chip MALDI-ToF mass spectrometry as a tool for characterising proteinaceous conditioning films on functionalised surfaces10.1016/j.aca.2013.10.007 ↗
26. Proteomic analysis for the assessment of different lots of fetal bovine serum as a raw material for cell culture. Part IV. Application of proteomics to the manufacture of biological drugs10.1021/bp060121o ↗
27. Comparison of nanotube-protein corona composition in cell culture media10.1002/smll.201202243 ↗
28. Significance of surface charge and shell material of superparamagnetic iron oxide nanoparticle (SPION) based core/shell nanoparticles on the composition of the protein corona10.1039/C4BM00264D ↗
29. Dispersion of nanoparticles in different media importantly determines the composition of their protein corona10.1371/journal.pone.0169552 ↗
30. ExPASy: SIB bioinformatics resource portal10.1093/nar/gks400 ↗
31. (2019, December 22). Available online: https://www.expasy.org/.
32. Practical quantitative biomedical applications of MALDI-TOF mass spectrometry10.1016/S1044-0305(02)00426-9 ↗
33. Water near bioinert self-assembled monolayers10.1038/s41428-018-0075-1 ↗
34. Mechanism underlying bioinertness of self-assembled monolayers of oligo(ethyleneglycol)-terminated alkanethiols on gold: protein adsorption, platelet adhesion, and surface forces10.1039/c2cp41236e ↗
35. Evaluation of Factors To Determine Platelet Compatibility by Using Self-Assembled Monolayers with a Chemical Gradient10.1021/acs.langmuir.5b01216 ↗
36. Molecular conformation in oligo(ethylene glycol)-terminated self-assembled monolayers on gold and silver surfaces determines their ability to resist protein adsorption10.1021/jp972635z ↗
37. Surface force and vibrational spectroscopic analyses of interfacial water molecules in the vicinity of methoxy-tri(ethylene glycol)-terminated monolayers: mechanisms underlying the effect of lateral packing density on bioinertness10.1080/09205063.2017.1303120 ↗
38. Nonfouling self-assembled monolayers: mechanisms underlying protein and cell resistance10.2174/1877946811101020090 ↗
39. Enhanced binding of Aspergillus fumigatus spores to A549 epithelial cells and extracellular matrix proteins by a component from the spore surface and inhibition by rat lung lavage fluid10.1136/thorax.55.7.579 ↗
40. Adsorption kinetics of protein mixtures. A tentative explanation of the Vroman effect10.1111/j.1749-6632.1987.tb33045.x ↗
41. Is the Vroman effect of importance in the interaction of blood with artificial materials?10.1163/156856292X00105 ↗
42. High-accuracy peptide mass fingerprinting using peak intensity data with machine learning10.1021/pr070088g ↗
43. Peak intensity prediction in MALDI-TOF mass spectrometry: a machine learning study to support quantitative proteomics10.1186/1471-2105-9-443 ↗
44. Peptide mass fingerprinting peak intensity prediction: extracting knowledge from spectra10.1002/1615-9861(200210)2:10<1374::AID-PROT1374>3.0.CO;2-D ↗
45. Universal metrics for quality assessment of protein identifications by mass spectrometry10.1074/mcp.M500426-MCP200 ↗