Labeling primary amine groups in peptides and proteins with N-hydroxysuccinimidyl ester modified Fe3O4@SiO2 nanoparticles containing cleavable disulfide-bond linkers

Bioconjugate Chemistry

Volumn 24, Issue 9, 2013, Pages 1562-1569

  Patil, Ujwal S ^a   Qu, Haiou ^a   Caruntu, Daniela ^a   O'Connor, Charles J ^a   Sharma, Arjun ^a,b   Cai, Yang ^a,b   Tarr, Matthew A ^a  

^a UNIVERSITY OF NEW ORLEANS   (United States)

^b CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BODY FLUIDS; CELL MEMBRANES; COVALENT BONDS; MAGNETIC SEPARATION; MAGNETITE; PEPTIDES; SILICA NANOPARTICLES; SULFUR COMPOUNDS;

DISULPHIDE BONDS; ESTER GROUPS; FUNCTIONALIZED; LABELINGS; LABELLED PROTEIN; PEPTIDE PROTEINS; PRIMARY AMINE GROUPS; PRIMARY AMINES; SILICA COATED; SUPERPARAMAGNETICS;

ESTERS;

AMINE; BOVINE SERUM ALBUMIN; ESTER DERIVATIVE; PEPTIDES AND PROTEINS; SUPERPARAMAGNETIC IRON OXIDE NANOPARTICLE;

ARTICLE; CELL SURFACE; CHEMICAL LABELING; CHEMICAL STRUCTURE; COLLISIONALLY ACTIVATED DISSOCIATION; CONJUGATION; DISULFIDE BOND; ELECTRON MICROSCOPY; ELECTROSPRAY MASS SPECTROMETRY; LIGHT SCATTERING; LIQUID CHROMATOGRAPHY; MAGNETIC SEPARATION; PROTEIN INTERACTION; ROOM TEMPERATURE; SYNTHESIS; TANDEM MASS SPECTROMETRY;

BOVINAE;

AMINES; ANIMALS; CATTLE; CHROMATOGRAPHY, LIQUID; DISULFIDES; MAGNETITE NANOPARTICLES; MODELS, MOLECULAR; PEPTIDES; SERUM ALBUMIN, BOVINE; SILICON DIOXIDE; STAINING AND LABELING; SUCCINIMIDES; TANDEM MASS SPECTROMETRY;

EID: 84884396388     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc400165r     Document Type: Article

References (47)

1. Hainfeld, J. F. and Powell, R. D. (2000) New frontiers in gold labeling J. Histochem. Cytochem. 48 (4) 471-480 (Pubitemid 30210350)
2. Neuberger, T., Bernhard, S., Hofmann, H., Hofmann, M., and Rechenberg, B. V. (2005) Superparamagnetic nanoparticles for biomedical applications: Possibilities and limitations of a new drug delivery system J. Magn. Magn. Mater. 293 (1) 483-496 (Pubitemid 40608969)
3. Safarik, I. and Safarikova, M. (2004) Magnetic techniques for the isolation and purification of proteins and peptides. Biomagn. Res. Technol. 2 (7) doi: 10.1186/1477-044X-2-7 (Pubitemid 44818551)
4. Hofmann, I., Schnolzer, M., Kaufmann, I., and Franke, W. W. (2002) Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes Mol. Biol. Cell 13 (5) 1665-1676 (Pubitemid 34522647)
5. Gao, M., Deng, C., and Zhang, X. (2011) Magnetic nanoparticles-based digestion and enrichment methods in proteomics analysis Expert. Rev. Proteomics 8 (3) 379-390
6. Laurent, S., Forge, D., Port, M., Roch, A., Robic, C., Vander Elst, L., and Muller, R. N. (2008) Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications Chem. Rev. 108 (6) 2064-2110
7. Li, Y. S., Church, J. S., Woodhead, A. L., and Moussa, F. (2010) Preparation and characterization of silica coated iron oxide magnetic nano-particles Spectrochim. Acta, Part A 76 (5) 484-489
8. Chen, W. Y. and Chen, Y. C. (2006) Affinity-based mass spectrometry using magnetic iron oxide particles as the matrix and concentrating probes for SALDI MS analysis of peptides and proteins Anal. Bioanal. Chem. 386 (3) 699-704
9. Di Marco, M., Shamsuddin, S., Razak, K. A., Aziz, A. A., Devaux, C., Borghi, E., Levy, L., and Sadun, C. (2010) Overview of the main methods used to combine proteins with nanosystems: absorption, bioconjugation, and encapsulation Int. J. Nanomed. 5, 37-49
10. Hermanson, G. T. (1996) Bioconjugate Techniques, pp 3-26, Chapter 1, Academic Press, San Diego.
11. Weber, C., Reiss, S., and Langer, K. (2000) Preparation of surface modified protein nanoparticles by introduction of sulfhydryl groups Int. J. Pharm. 211 (1-2) 67-78 (Pubitemid 32008385)
12. Gurd, F. R. N. (1967) Methods in Enzymology (Hirs, C. H. W., Ed.) pp 532-541, Vol. 11, Academic Press, New York.
13. Heitz, J. R., Anderson, C. D., and Anderson, B. M. (1968) Inactivation of yeast alcohol dehydrogenase by N-alkylmaleimides Arch. Biochem. Biophys. 127, 627-636
14. Ross, W. C. J. (1953) The chemistry of cytotoxic alkylating agents Adv. Cancer Res. 1, 397
15. King, T. P., Li, Y., and Kochoumian, L. (1978) Preparation of protein conjugates via intermolecular disulfide bond formation Biochemistry 17 (8) 1499-1506 (Pubitemid 8330387)
16. 2 nanoparticles: Application to comprehensive proteomic profiling J. Proteome Res. 7 (8) 3591-3596
17. Herriott, R. M. (1947) Reactions of native proteins with chemical reagents Adv. Protein Chem. 3, 169-225
18. Riehm, J. P. and Scheraga, H. A. (1965) Structural studies of ribonuclease. XVII. A reactive carboxyl group in ribonuclease Biochemistry 4, 772-782
19. Anderson, G. W. and Paul, Rolf (1958) N,N′-carbonyldiimidazole, a new regent for peptide synthesis J. Am. Chem. Soc. 80 (16) 4423-4423
20. Hoare, D. G. and Koshland, D. E. (1966) A procedure for the selective modification of carboxyl groups in proteins J. Am. Chem. Soc. 88 (9) 2057-2058
21. Brunswick, M., Finkelman, F. D., Highet, P. F., Inman, J. K., Dintzis, H. M., and Mond, J. J. (1988) Picogram quantities of anti-Ig antibodies coupled to dextran induce B cell proliferation J. Immunol. 140 (10) 3364-3372
22. Annunziato, M. E. P., Usha, S., Ranade, M., and Palumbo, P. S. (1993) p-Maleimidophenyl isocyanate: a novel heterobifunctional linker for hydroxyl to thiol coupling Bioconjugate Chem. 4 (3) 212-218
23. Geoghegan, K. F. and Stroh, J. G. (1992) Site-directed conjugation of nonpeptide groups to peptides and proteins via periodate oxidation of a 2-amino alcohol. Application to modification at N-terminal serine Bioconjugate Chem. 3 (2) 138-146
24. Cheng, K., El-Boubbou, Kheireddine, L., and Christopher, C. (2011) Binding of HIV-1 gp120 glycoprotein to silica nanoparticles modified with CD4 glycoprotein and CD4 peptide fragments ACS Appl. Mater. Interfaces 4 (1) 235-243
25. Qian, J., Cole, R. B., and Cai, Y. (2011) Synthesis and characterization of a 'fluorous' (fluorinated alkyl) affinity reagent that labels primary amine groups in proteins/peptides J. Mass. Spectrom. 46 (1) 1-11
26. Zhao, L. Y., Zhang, Y. J., Wei, J. Y., Cao, D., Liu, K. H., and Qian, X. H. (2009) A rapid isolation and identification method for blocked N-terminal peptides by isothiocyanate-coupled magnetic nanoparticles and MS Proteomics 9 (18) 4416-4420
27. Rifai, A. and Wong, S. S. (1986) Preparation of phosphorylcholine- conjugated antigens J. Immunol. Methods 94 (1-2) 25-30 (Pubitemid 17186340)
28. Voet, D., Voet, J. G., and Pratt, C. W. (2008) Fundamentals of Biochemistry: Life at the Molecular Level, 3 rd ed., Wiley & Sons, Inc. Press, New York.
29. Kerr, T. J. and McLean, J. A. (2010) Peptide quantitation using primary amine selective metal chelation labels for mass spectrometry Chem. Commun. 46 (30) 5479-5481
30. Nicolardi, S., Andreoni, A., Tabares, L. C., van der Burgt, Y. E., Canters, G. W., Deelder, A. M., and Hensbergen, P. J. (2012) Top-down FTICR MS for the identification of fluorescent labeling efficiency and specificity of the Cu-protein azurin Anal. Chem. 84 (5) 2512-2520
31. Wu, J., Liu, W., Sousa, E., Qiu, Y., Pittman, D. D., Maganti, V., Feldman, J., Gill, D., Lu, Z., Dorner, A. J., Schaub, R., and Tan, X. Y. (2007) Proteomic identification of endothelial proteins isolated in situ from atherosclerotic aorta via systemic perfusion J. Proteome Res. 6 (12) 4728-4736
32. Lee, S. J., Kim, K. H., Park, J. S., Jung, J. W., Kim, Y. H., Kim, S. K., Kim, W. S., Goh, H. G., Kim, S. H., Yoo, J. S., Kim, D. W., and Kim, K. P. (2007) Comparative analysis of cell surface proteins in chronic and acute leukemia cell lines Biochem. Biophys. Res. Commun. 357 (3) 620-626 (Pubitemid 46653824)
33. Zhang, Y., Li, W., Ou, L., Wang, W., Delyagina, E., Lux, C., Sorg, H., Riehemann, K., Steinhoff, G., and Ma, N. (2012) Targeted delivery of human VEGF gene via complexes of magnetic nanoparticle-adenoviral vectors enhanced cardiac regeneration PLoS One 7 (7) e39490
34. Niehage, C., Steenblock, C., Pursche, T., Bornhauser, M., Corbeil, D., and Hoflack, B. (2011) The cell surface proteome of human mesenchymal stromal cells PLoS One 6 (5) e20399
35. Sears, K. T., Ceraul, S. M., Gillespie, J. J., Allen, E. D., Jr., Popov, V. L., Ammerman, N. C., Rahman, M. S., and Azad, A. F. (2012) Surface proteome analysis and characterization of surface cell antigen (Sca) or autotransporter family of Rickettsia typhi PLoS Pathog. 8 (8) e1002856
36. Masuoka, J., Guthrie, L. N., and Hazen, K. C. (2002) Complications in cell-surface labelling by biotinylation of Candida albicans due to avidin conjugate binding to cell-wall proteins Microbiology 148 (4) 1073-1079 (Pubitemid 34436782)
37. Cronan, J. E., Jr. (1990) Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins J. Biol. Chem. 265 (18) 10327-10333
38. Piercenet NHS-Activated Magnetic Beads http://www.piercenet.com/browse. cfm?fldID=0F8DD229-E208-E8DE-6EBD-762CA089E687.
39. Liu, Q., Xu, Z., Finch, J. A., and Egerton, R. (1998) A novel two-step silica-coating process for engineering magnetic nanocomposites Chem. Mater. 10 (12) 3936-3940 (Pubitemid 128657916)
40. Huang, Y. F., Wang, Y. F., and Yan, X. P. (2010) Amine-functionalized magnetic nanoparticles for rapid capture and removal of bacterial pathogens Environ. Sci. Technol. 44 (20) 7908-13
41. Kumar, C. S. S. R. (2009) Magnetic Nanomaterials, Vol. 4, Wiley-VCH Verlag GmbH and Co KGaA, Weinheim.
42. Shen, X.-C., Fang, X. Z., Zhou, Y. H., and Liang, H. (2004) Synthesis and characterization of 3-aminopropyltriethoxysilane-modified superparamagnetic magnetite nanoparticles Chem. Lett. 33 (11) 1468-1469 (Pubitemid 40221362)
43. Yamaura, M., Camilo, R. L., Sampaio, L. C., Maceîdo, M. A., Nakamura, M., and Toma, H. E. (2004) Preparation and characterization of (3-aminopropyl)triethoxysilane-coated magnetite nanoparticles J. Magn. Magn. Mater. 279 (2-3) 210-217
44. Carlsson, J., Drevin, H., and Axen, R. (1978) Protein thiolation and reversible protein-protein conjugation. N-Succinimidyl 3-(2-pyridyldithio) propionate, a new heterobifunctional reagent Biochem. J. 173 (3) 723-737 (Pubitemid 9010965)
45. Proteinprospector v 5.10.9; http://prospector.ucsf.edu/prospector/mshome. htm.
46. Majorek, K. A., Porebski, P. J., Dayal, A., Zimmerman, M. D., Jablonska, K., Stewart, A. J., Chruszcz, M., and Minor, W. (2012) Structural and immunologic characterization of bovine, horse, and rabbit serum albumins Mol. Immunol. 52 (3-4) 174-182
47. Brown, J. R. (1974) Structure of serum albumin: disulfide bridges Fed. Proc. 33, 1389-1389