journal article·2015-03-01

Analysis of protein coatings on gold nanoparticles by XPS and liquid-based particle sizing techniques

Natalie A. Belsey, Alex G. Shard, Caterina Minelli

Biointerphases· Volume 10· Issue 1
Publisher page

Abstract

The precise use of nanoparticles in technological applications requires control over their surface properties. This implies the ability to quantitatively describe, for example, molecular coatings in terms of their thickness, areal mass, or number of molecules. Here, the authors describe two different approaches to the measurement of these parameters by using gold nanoparticles ranging in diameter from 10 to 80 nm and coated with three different proteins: immunoglobulin G, bovine serum albumin, and a peptide. One approach utilizes ultraviolet–visible spectroscopy, dynamic light scattering, and differential centrifugal sedimentation to measure the protein shell refractive indices and thicknesses, from which the number of molecules in the protein shell can be derived. The other approach employs x-ray photoelectron spectroscopy to measure the thickness of the dry molecular coatings and also to derive the number of molecules in the protein shell. The authors demonstrate that the two approaches, although very different, produce consistent measurement results. This finding is important to extend the quantitative analysis of nanoparticle molecular coatings to a wide range of materials.
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Research context

OpenAlex topics: Polymer Surface Interaction Studies · Nanoparticle-Based Drug Delivery · Gold and Silver Nanoparticles Synthesis and Applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Analytical Science National Physical Laboratory, , Hampton Road, Teddington, Middlesex TW11 0LW, United Kingdom

References (40)

Show source-provided references
1. Small · 2010 · 6 · 233610.1002/smll.201000523 ↗
2. Nano Lett. · 2003 · 3 · 93510.1021/nl034223+ ↗
3. J. Biosci. Bioeng. · 2005 · 100 · 110.1263/jbb.100.1 ↗
4. Anal. Chem. · 2009 · 81 · 160010.1021/ac802345z ↗
5. J. Am. Chem. Soc. · 2004 · 126 · 593210.1021/ja049384+ ↗
6. Nat. Nanotechnol. · 2012 · 7 · 77910.1038/nnano.2012.207 ↗
7. Nat. Nanotechnol. · 2013 · 8 · 77210.1038/nnano.2013.181 ↗
8. Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: A review10.1016/j.aca.2014.10.031 ↗
9. Nat. Rev. Drug Discovery · 2010 · 9 · 61510.1038/nrd2591 ↗
10. Anal. Methods · 2013 · 5 · 459110.1039/c3ay40771c ↗
11. Surf. Interface Anal. · 2014 · 46 · 66310.1002/sia.5381 ↗
12. Langmuir · 2012 · 28 · 1086010.1021/la301351k ↗
13. Anal. Chem. · 2011 · 83 · 865910.1021/ac202110x ↗
14. J. Am. Chem. Soc. · 2013 · 135 · 1504010.1021/ja404346p ↗
15. Anal. Chem. · 2011 · 83 · 670410.1021/ac201175a ↗
16. Biointerphases · 2011 · 6 · 9810.1116/1.3622481 ↗
17. Surf. Interface Anal. · 2013 · 45 · 173710.1002/sia.5315 ↗
18. J. Phys. Chem. C · 2012 · 116 · 1680610.1021/jp305267d ↗
19. Nat. Mater. · 2002 · 1 · 16910.1038/nmat758 ↗
20. 1983
21. C. Mätzler, Research Report No. 2002-08, Institut für Angewandte Physik, University of Bern (2002), available at http://arrc.ou.edu/~rockee/NRA_2007_website/Mie-scattering-Matlab.pdf.
22. J. Teichroeb, “Selected experiments with proteins at solid-liquid interfaces,” Ph.D. thesis (University of Waterloo, Canada, 2008).
23. See supplementary material at http://dx.doi.org/10.1116/1.4913566 for analysis of protein coatings on gold nanoparticles by XPS and liquid-based particle sizing techniques.
24. J. Electron Spectrosc. Relat. Phenom. · 2001 · 120 · 9310.1016/S0368-2048(01)00311-5 ↗
25. J. Colloid Interface Sci. · 2013 · 405 · 32210.1016/j.jcis.2013.02.030 ↗
26. J. Am. Chem. Soc. · 2007 · 129 · 415610.1021/ja0706504 ↗
27. Langmuir · 2005 · 21 · 930310.1021/la050588t ↗
28. ACS Nano · 2013 · 7 · 888110.1021/nn403350v ↗
29. Langmuir · 2010 · 26 · 1274010.1021/la100761f ↗
30. Colloid Surf. B · 1995 · 5 · 1110.1016/0927-7765(95)98205-2 ↗
31. Langmuir · 2011 · 28 · 273610.1021/la203528u ↗
32. Anal. Chim. Acta · 2010 · 675 · 19110.1016/j.aca.2010.07.016 ↗
33. Biophys. J. · 2001 · 80 · 242210.1016/S0006-3495(01)76211-X ↗
34. Langmuir · 2012 · 28 · 911310.1021/la300402w ↗
35. PNAS · 1951 · 37 · 72910.1073/pnas.37.11.729 ↗
36. Biophys. J. · 2004 · 87 · 55310.1529/biophysj.103.030072 ↗
37. Biopolymers · 1978 · 17 · 175910.1002/bip.1978.360170711 ↗
38. Biophys. J. · 2011 · 100 · 230910.1016/j.bpj.2011.03.004 ↗
39. Protein Sci. · 2004 · 13 · 282510.1110/ps.04688204 ↗
40. Appl. Phys. Lett. · 2014 · 104 · 24310610.1063/1.4884065 ↗