Measuring protein isoelectric points by AFM-based force spectroscopy using trace amounts of sample

Nature Nanotechnology

Volumn 11, Issue 9, 2016, Pages 817-823

  Guo, Shifeng ^a   Zhu, Xiaoying ^a,f   Jańczewski, Dominik ^a,b   Lee, Serina Siew Chen ^c   He, Tao ^a   Teo, Serena Lay Ming ^c   Vancso, G Julius ^d,e  

^a INSTITUTE OF MATERIALS RESEARCH AND ENGINEERING   (Singapore)

^b WARSAW UNIVERSITY OF TECHNOLOGY   (Poland)

^c NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^d INSTITUTE OF CHEMICAL AND ENGINEERING SCIENCES   (Singapore)

^e UNIVERSITY OF TWENTE   (Netherlands)

^f ZHEJIANG UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIVES; ATOMIC FORCE MICROSCOPY; BODY FLUIDS; DEPOSITION; MAMMALS; POLYELECTROLYTES;

BOVINE SERUM ALBUMINS; CONVENTIONAL METHODS; FORCE SPECTROSCOPY; FORCE-DISTANCE CURVES; ISOELECTRIC POINT (PI); LAYER BY LAYER DEPOSITION; NEGATIVELY CHARGED; PROTEIN ISOELECTRIC POINTS;

PROTEINS;

BOVINE SERUM ALBUMIN; FIBRINOGEN; GLUTARALDEHYDE; MYOGLOBIN; POLYELECTROLYTE; RIBONUCLEASE A; SURFACE WATER; IMMOBILIZED PROTEIN;

ADHESION; AMPHIBALANUS AMPHITRITE; ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; FORCE; HYDROPHILICITY; ISOELECTRIC POINT; LARVA; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN IMMOBILIZATION; PROTEIN INTERACTION; PROTEIN ISOELECTRIC POINT; STATIC ELECTRICITY; SURFACE CHARGE; SURFACE PROPERTY; ZETA POTENTIAL; ANIMAL; BARNACLE; BOVINE; CHEMISTRY; PH; PROCEDURES;

ANIMALS; CATTLE; HYDROGEN-ION CONCENTRATION; IMMOBILIZED PROTEINS; ISOELECTRIC POINT; MICROSCOPY, ATOMIC FORCE; SERUM ALBUMIN, BOVINE; SURFACE PROPERTIES; THORACICA;

EID: 84979515519     PISSN: 17483387     EISSN: 17483395     Source Type: Journal    
DOI: 10.1038/nnano.2016.118     Document Type: Article

References (48)

1. Righetti, P. G. & Caravaggio, T. Isoelectric points and molecular weights of proteins: a table. J. Chromatogr. A 127, 1-28 (1976).
2. Hughes, A. J., Tentori, A. M. & Herr, A. E. Bistable isoelectric point photoswitching in green fluorescent proteins observed by dynamic immunoprobed isoelectric focusing. J. Am. Chem. Soc. 134, 17582-17591 (2012).
3. Righetti, P. G. Determination of the isoelectric point of proteins by capillary isoelectric focusing. J. Chromatogr. A 1037, 491-499 (2004).
4. Mohan, D. & Lee, C. S. Extension of separation range in capillary isoelectric focusing for resolving highly basic biomolecules. J. Chromatogr. A 979, 271-276 (2002).
5. Shen, Y. & Smith, R. D. Proteomics based on high-efficiency capillary separations. Electrophoresis 23, 3106-3124 (2002).
6. Righetti, P. G., Gelfi, C. & Conti, M. Protein purification: principles, high resolution methods, and applications. J. Chromatogr. B 699, 91-104 (1997).
7. Pihlasalo, S., Auranen, L., Hanninen, P. & Harma, H. Method for estimation of protein isoelectric point. Anal. Chem. 84, 8253-8258 (2012).
8. Callow, J. A. & Callow, M. E. Trends in the development of environmentally friendly fouling-resistant marine coatings. Nature Commun. 2, 244 (2011).
9. Smith, C. Striving for purity: advances in protein purification. Nature Methods 2, 71-77 (2005).
10. De, M. et al. Sensing of proteins in human serum using conjugates of nanoparticles and green fluorescent protein. Nature Chem. 1, 461-465 (2009).
11. Yan, J. et al. Effect of proteins with different isoelectric points on the gene transfection efficiency mediated by stearic acid grafted chitosan oligosaccharide micelles. Mol. Pharm. 10, 2568-2577 (2013).
12. Butt, H. J., Cappella, B. & Kappl, M. Force measurements with the atomic force microscope: technique, interpretation and applications. Surf. Sci. Rep. 59, 1-152 (2005).
13. Lee, H., Scherer, N. F. & Messersmith, P. B. Single-molecule mechanics of mussel adhesion. Proc. Natl Acad. Sci. USA 103, 12999-13003 (2006).
14. Beaussart, A. et al. Quantifying the forces guiding microbial cell adhesion using single-cell force spectroscopy. Nature Protocols 9, 1049-1055 (2014).
15. Xu, L. C. & Siedlecki, C. A. Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces. Biomaterials 28, 3273-3283 (2007).
16. Yersin, A. et al. Interactions between synaptic vesicle fusion proteins explored by atomic force microscopy. Proc. Natl Acad. Sci. USA 100, 8736-8741 (2003).
17. Vezenov, D. V., Noy, A., Rozsnyai, L. F. & Lieber, C. M. Force titrations and ionization state sensitive imaging of functional groups in aqueous solutions by chemical force microscopy. J. Am. Chem. Soc. 119, 2006-2015 (1997).
18. Ahimou, F., Denis, F. A., Touhami, A. & Dufrêne, Y. F. Probing microbial cell surface charges by atomic force microscopy. Langmuir 18, 9937-9941 (2002).
19. Zhu, X. et al. Polyion multilayers with precise surface charge control for antifouling. ACS Appl. Mater. Interfaces 7, 852-861 (2015).
20. Zhu, X., Jańczewski, D., Lee, S. S. C., Teo, S. L. M. & Vancso, G. J. Cross-linked polyelectrolyte multilayers for marine antifouling applications. ACS Appl. Mater. Interfaces 5, 5961-5968 (2013).
21. Barattin, R. & Voyer, N. Chemical modifications of AFM tips for the study of molecular recognition events. Chem. Commun. 13, 1513-1532 (2008).
22. Patel, A. B. et al. Influence of architecture on the kinetic stability of molecular assemblies. J. Am. Chem. Soc. 126, 1318-1319 (2004).
23. Steiner, P. et al. Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and recycling of the glutamate receptor subunit GluR2. EMBO J. 24, 2873-2884 (2005).
24. Roach, P., Farrar, D. & Perry, C. C. Interpretation of protein adsorption: surfaceinduced conformational changes. J. Am. Chem. Soc. 127, 8168-8173 (2005).
25. Rabe, M., Verdes, D. & Seeger, S. Understanding protein adsorption phenomena at solid surfaces. Adv. Colloid Interface Sci. 162, 87-106 (2011).
26. Liu, H. & Hu, N. Interaction between myoglobin and hyaluronic acid in their layer-by-layer assembly: quartz crystal microbalance and cyclic voltammetry studies. J. Phys. Chem. B 110, 14494-14502 (2006).
27. Belfort, G. & Lee, C. S. Attractive and repulsive interactions between and within adsorbed ribonuclease A layers. Proc. Natl Acad. Sci. USA 88, 9146-9150 (1991).
28. Merkel, R., Nassoy, P., Leung, A., Ritchie, K. & Evans, E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397, 50-53 (1999).
29. Gergely, C. et al. Unbinding process of adsorbed proteins under external stress studied by atomic force microscopy spectroscopy. Proc. Natl Acad. Sci. USA 26, 10802-10807 (2000).
30. Noy, A., Frisbie, C. D., Rozsnyai, L. F., Wrighton, M. S. & Lieber, C. M. Chemical force microscopy: exploiting chemically-modified tips to quantify adhesion, friction, and functional group distributions in molecular assemblies. J. Am. Chem. Soc. 117, 7943-7951 (1995).
31. Frisbie, C. D., Rozsnyai, L. F., Noy, A., Wrighton, M. S. & Lieber, C. M. Functional group imaging by chemical force microscopy. Science 265, 2071-2073 (1994).
32. Cappella, B. & Dietler, G. Force-distance curves by atomic force microscopy. Surf. Sci. Rep. 34, 1-104 (1999).
33. Sui, X., Chen, Q., Hempenius, M. A. & Vancso, G. J. Probing the collapse dynamics of poly(N-isopropylacrylamide) brushes by AFM: effects of co-nonsolvency and grafting densities. Small 7, 1440-1447 (2011).
34. Erikson, H. P. Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol. Proced. Online 11, 32-51 (2009).
35. Guo, S. et al. Barnacle larvae exploring surfaces with variable hydrophilicity: influence of morphology and adhesion of 'footprint' proteins by AFM. ACS Appl. Mater. Interfaces 6, 13667-13676 (2014).
36. Neihof, R. A. & Loeb, G. I. The surface charge of particulate matter in seawater. Limnol. Oceanogr. 17, 7-16 (1972).
37. Rosenberg, M. & Kjelleberg, S. Hydrophobic interactions: role in bacterial adhesion. Adv. Microb. Ecol. 9, 353-393 (1986).
38. Shi, H., Liu, J., Geng, J., Tang, B. Z. & Liu, B. Specific detection of integrin αvβ3 by light-up bioprobe with aggregation-induced emission characteristics. J. Am. Chem. Soc. 134, 9569-9572 (2012).
39. Barua, S. et al. Particle shape enhances specificity of antibody-displaying nanoparticles. Proc. Natl Acad. Sci. USA 110, 3270-3275 (2013).
40. Zhu, G., Mallery, S. R. & Schwendeman, S. P. Stabilization of proteins encapsulated in injectable poly (lactide-co-glycolide). Nature Biotechnol. 18, 52-57 (2000).
41. Wasilewska, M., Adamczyk, Z. & Jachimska, B. Structure of fibrinogen in electrolyte solutions derived from dynamic light scattering (DLS) and viscosity measurements. Langmuir 25, 3698-3704 (2009).
42. Scheraga, H. A. & Laskowski, M. J. The fibrinogen-fibrin conversion. Adv. Protein. Chem. 12, 1-131 (1957).
43. Caulfield, J. P. & Farquhar, M. G. Distribution of anionic sites in glomerular basement membranes: their possible role in filtration and attachment. Proc. Natl Acad. Sci. USA 73, 1646-1650 (1976).
44. Liu, Q. et al. Graphene and graphene oxide sheets supported on silica as versatile and high-performance adsorbents for solid-phase extraction. Angew. Chem. Int. Ed. 123, 6035-6039 (2011).
45. Wright, A. T. & Anslyn, E. A. Differential receptor arrays and assays for solutionbased molecular recognition. Chem. Soc. Rev. 35, 14-28 (2006).
46. Wang, C. & Lucy, C. A. Oligomerized phospholipid bilayers as semipermanent coatings in capillary electrophoresis. Anal. Chem. 77, 2015-2021 (2005).
47. Ravindra, R., Zhao, S., Gies, H. & Winter, R. Protein encapsulation in mesoporous silicate: the effects of confinement on protein stability, hydration, and volumetric properties. J. Am. Chem. Soc. 126, 12224-12225 (2004).
48. Hutter, J. L. & Bechhoefer, J. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64, 1868-1873 (1993).