Comparison of nanowire pellicles for plasma membrane enrichment: coating nanowires on cell
Source abstract
Abstract
A study is reported on the effect of nanowire density on the ease of pellicle formation and the enrichment of plasma membrane proteins for analysis by mass spectrometry. An optimized synthesis is reported for iron silicate nanowires with a narrow size range of 900 ±400 nm in length and 200 nm diameter. The nanowires were coated with Al2O3 and used to form pellicles around suspended multiple myeloma cells, which acted as a model for cells recovered from tissue samples. Lighter alumina-coated silica nanowires were also synthesized (Kim et al. 2013), which allowed a comparison of the construction of the two pellicles and of the effect of nanowire density on plasma membrane enrichment. Evidence is offered that the dense nanowire pellicle does not crush or distort these mammalian cells. Finally, the pellicles were incorporated into a mass-spectrometry-based proteomic workflow to analyze transmembrane proteins in the plasma membrane. In contrast to a prior comparison of the effect of density with nanoparticles pellicles (Choksawangkarn et al. 2013), nanowire density was not found to significantly affect the enrichment of the plasma membrane. However, nanowires with a favorable aspect for pellicle formation are more easily and reliably produced with iron silicate than with silica. Additionally, the method for pellicle formation was optimized through the use of iron silicate nanowires (ISNW), which is crucial to the improvement of PM protein enrichment and analysis.
Source: europepmc · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Advanced Proteomics Techniques and Applications · Advanced biosensing and bioanalysis techniques · Monoclonal and Polyclonal Antibodies Research
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (17)
Show source-provided references
1. Ashburner M, Ball CA, Blake JA, Botstein D, Butler H, Cherry JM, Davis PA, Dolinski K, Dwight SS, Eppig JT, Harris MA, Hill DP, Issel-Tarver L, Kasarskis A, Lewis S, Matese JC, Richardson JE, Ringwald M, Rubin GM, Sherlock G (2009) Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat Genet 25:25–29. doi: 10.1038/7555610.1038/75556 ↗
2. Blackler AR, Speers AE, Ladinsky MS, Wu CC (2008) A shotgun proteomic method for the identification of membrane-embedded proteins and peptides. J Proteome Res 7:3028–3034. doi: 10.1021/pr700795f10.1021/pr700795f ↗
3. Chaney LK, Jacobson BS (1983) Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins. J Biol Chem 258:10062–1007210.1016/S0021-9258(17)44606-0 ↗
4. Choksawangkarn W, Kim SK, Cannon JR, Edwards NJ, Lee SB, Fenselau C (2013) Enrichment of plasma membrane proteins using nanoparticle pellicles: comparison between silica and higher density nanoparticles. J Proteome Res 12:1134–1141. doi: 10.1021/pr301107x10.1021/pr301107x ↗
5. Edwards N, Wu X, Tseng TW (2009) An unsupervised, model-free, machine-learning combiner for peptide identifications from tandem mass spectra. Clin Proteomics 5:23–36. doi: 10.1007/s12014-009-9024-510.1007/s12014-009-9024-5 ↗
6. Elschenbroich S, Kim Y, Medin JA, Kislinger T (2010) Isolation of cell surface proteins for mass spectrometry-based proteomics. Expert Rev Proteomics 7:141–154. doi: 10.1586/epr.09.9710.1586/epr.09.97 ↗
7. Kim SK, Choksawangkarn W, Rose R, Fenselau C, Lee SB (2013) Nanowire pellicles for eukaryotic cells: nanowire coating and interaction with cells. Nanomedicine. doi: 10.2217/NNM.13.9610.2217/nnm.13.96 ↗
8. Li X, Jia X, Xie C, Lin Y, Cao R, He Q, Chen P, Wang X, Liang S (2009a) Development of cationic colloidal silica-coated magnetic nanospheres for highly selective and rapid enrichment of plasma membrane fractions for proteomics analysis. Biotechnol Appl Biochem 54:213–220. doi: 10.1042/BA2009018710.1042/BA20090187 ↗
9. Li X, Jin X, Cao J, Xie C, Cao R, Liu Z, Xiong J, Li J, Yang X, Chen P, Liang S (2009b) Evaluation of two cell surface modification methods for proteomic analysis of plasma membrane from isolated mouse hepatocytes. Biochim Biophys Acta 1794:32–41. doi: 10.1016/j.bbapap.2008.07.00910.1016/j.bbapap.2008.07.009 ↗
10. Overington JP, Al-Lazikzni B, Hopkins AL (2006) How many drug targets are there? Nat Rev Drug Discov 5:993–996. doi: 10.1038/nrd219910.1038/nrd2199 ↗
11. Prior MJ, Larance M, Lawrence RT, Soul J, Humphrey S, Burchfield J, Kistler C, Davey JR, La-Borde PJ, Buckley M, Kanazawa H, Parton RG, Guihaus M, James DE (2011) Quantitative proteomic analysis of the adipocyte plasma membrane. J Proteome Res 10:4970–4982. doi: 10.1021/pr200446r10.1021/pr200446r ↗
12. Rahbar AM, Fenselau C (2004) Integration of Jacobson’s pellicle method into proteomic strategies for plasma membrane proteins. J Proteome Res 3:1267–1277. doi: 10.1021/pr040004t10.1021/pr040004t ↗
13. Rahbar AM, Fenselau C (2005) Unbiased examination of changes in plasma membrane proteins in drug resistant cancer cells. J Proteome Res 4:2148–2153. doi: 10.1021/pr050237010.1021/pr0502370 ↗
14. Speers AE, Wu CC (2007) Proteomics of integral membrane proteins: theory and application. Chem Rev 107:3687–371410.1021/cr068286z ↗
15. Wessel D, Flugge UI (1984) A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal Biochem 138:141–143. doi: 10.1016/0003-2697(84)90782-610.1016/0003-2697(84)90782-6 ↗
16. Wu C, Yates JR (2003) The application of mass spectrometry to membrane proteomics. Nat Biotechnol 21:262–26710.1038/nbt0303-262 ↗
17. Zhang W, Zhao C, Wang S, Fang C, Xu Y, Lu H, Yang P (2011) Coating cells with cationic silica-magnetite nanocomposites for rapid purification of integral plasma membrane proteins. Proteomics 11:3482–3490. doi: 10.1002/pmic.20100021110.1002/pmic.201000211 ↗