Abstract
In proteome research, rapid and effective separation strategies are essential for successful protein identification due to the broad dynamic range of proteins in biological samples. Some important proteins are often expressed in ultra low abundance, thus making the pre-concentration procedure before mass spectrometric analysis prerequisite. The main purpose of enrichment is to isolate target molecules from complex mixtures to reduce sample complexity and facilitate the subsequent analyzing steps. The introduction of nanoparticles into this field has accelerated the development of enrichment methods. In this review, we mainly focus on recent developments of using different nanomaterials for pre-concentration of low-abundance peptides/ proteins, including those containing post-translational modifications, such as phosphorylation and glycosylation, prior to mass spectrometric analysis.
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Fields S. Proteomics in genomeland. Science, 2001, 291(5507): 1221–1224
Anderson NL, Anderson NG. The human plasma proteome. Mol Cell Proteomics, 2002, 1(11): 845–867
Corthals GL, Wasinger VC, Hochstrasser DF, Sanchez JC. The dynamic range of protein expression: a challenge for proteomic research. Electrophoresis, 2000, 21(6): 1104–1115
Gao M, Deng C, Yu W, Zhang Y, Yang P, Zhang X. Large scale depletion of the high-abundance proteins and analysis of middle- and low-abundance proteins in human liver proteome by multidimensional liquid chromatography. Proteomics, 2008, 8(5): 939–947
Zhang LJ, Lu HJ, Yang PY. Development of preconcentration for mass spectrometry in proteomics. Chin J Anal Chem, 2007, 35(1): 146–152
Alivisatos P. The use of nanocrystals in biological detection. Nat Biotechnol, 2004, 22(1): 47–52
Niemeyer CM. Nanoparticles, proteins, and nucleic Acids: Biotechnology meets materials science. Angew Chem Int Ed, 2001, 40(22): 4128–4158
Jun YW, Lee JH, Cheon J. Chemical design of nanoparticle probes for high-performance magnetic resonance imaging. Angew Chem Int Ed, 2008, 47(28): 5122–5135
Santra S, Dutta D, Walter GA, Moudgil BM. Fluorescent nanoparticle probes for cancer imaging. Technol Cancer Res T, 2005, 4(6): 593–601
Dobson J. Gene therapy progress and prospects: magnetic nanoparticle-based gene delivery. Gene Ther, 2006, 13(4): 283–287
Yoon TJ, Kim JS, Kim BG, Yu KN, Cho MH, Lee JK. Multifunctional nanoparticles possessing a “magnetic motor effect” for drug or gene delivery. Angew Chem Int Ed, 2005, 44(7): 1068–1071
Nasongkla N, Bey E, Ren J, Ai H, Khemtong C, Guthi JS, Chin SF, Sherry AD, Boothman DA, Gao J. Multifunctional polymeric micelles as cancer-targeted, MRI-ultrasensitive drug delivery dystems. Nano Lett, 2006, 6(11): 2427–2430
You CC, Miranda OR, Gider B, Ghosh PS, Kim IB, Erdogan B, Krovi SA, Bunz UHF, Rottello VM. Detection and identification of proteins using nanoparticle-fluorescent polymer “chemical nose” sensors. Nat Nanotechnol, 2007, 2(5): 318–323
You CC, Chompoosor A, Rotello VM. The biomacromoleculenanoparticle interface. Nano Today, 2007, 2(3): 34–43
Hicks JF, Zamborini FP, Osisek AJ, Murray RW. The dynamics of electron self-exchange between nanoparticles. J Am Chem Soc, 2001, 123(29): 7048–7053
Hicks JF, Miles DT, Murray RW. Quantized double-layer charging of highly monodisperse metal nanoparticles. J Am Chem Soc, 2002, 124(44): 13322–13328
Skaff H, Sill K, Emrick T. Quantum dots tailored with poly(paraphenylene vinylene). J Am Chem Soc, 2004, 126(36): 11322–11325
Redl FX, Black CT, Papaefthymiou GC, Sandstrom RL, Yin M, Zeng H, Murray CB, O’Brien SP. Magnetic, electronic, and structural characterization of nonstoichiometric iron oxides at the nanoscale. J Am Chem Soc, 2004, 126(44): 14583–14599
Park HG. Nanoparticle-based detection technology for DNA analysis. Biotechnol Bioprocess Eng, 2003, 8(4): 221–226
Zheng M, Huang X. Nanoparticles comprising a mixed monolayer for specific bindings with biomolecules. J Am Chem Soc, 2004, 126(38): 12047–12054
Dutta D, Sundaram SK, Teeguarden JG, Riley BJ, Fifield LS, Jacobs JM, Addleman SR, Kaysen GA, Moudgil BM, Weber TJ. Adsorbed proteins influence the biological activity and molecular targeting of nanomaterials. Toxicol Sci, 2007, 100(1): 301–315
Kaufman ED, Belyea J, Johnson MC, Nicholson ZM, Ricks JL, Shah PK, Bayless M, Pettersson T, Feldotö Z, Blomberg E, Claesson P, Franzen S. Probing protein adsorption onto mercaptoundecanoic acid stabilized gold nanoparticles and surfaces by quartz crystal microbalance and zeta-potential measurements. Langmuir, 2007, 23(11): 6053–6062
Cedervall T, Lynch I, Foy M, Berggård T, Donnelly SC, Cagney G, Linse S, Dawson KA. Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew Chem Int Ed, 2007, 46(30): 5754–5756
Lindman S, Lynch I, Thulin E, Nilsson H, Dawson KA, Linse S. Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity. Nano Lett, 2007, 7(4): 914–920
Cedervall T, Lynch S, Lindman S, Berggård T, Thulin E, Nilsson H, Dawson KA, Linse S. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA, 2007, 104(7): 2050–2055
Lynch I, Dawson KA. Protein-nanoparticle interactions. Nano Today, 2008, 3(12): 40–47
Fischer NO, Mclintosh CM, Simard JM, Rotello VM. Inhibition of chymotrypsin through surface binding using nanoparticle-based receptors. Proc Natl Acad Sci USA, 2002, 99(8): 5018–5023
Lin CC, Yeh YC, Yang CY, Chen CL, Chen GF, Chen CC, Wu YC. Selective binding of mannose-encapsulated gold nanoparticles to type 1 pili in Escherichia coli. J Am Chem Soc, 2002, 124(14): 3508–3509
Zheng M, Davidson F, Huang X. Ethylene glycol monolayer protected nanoparticles for eliminating nonspecific binding with biological molecules. J Am Chem Soc, 2003, 125(26): 7790–7791
Xu C, Xu K, Gu H, Zhong X, Guo Z, Zheng R, Zhang X, Xu B. Nitrilotriacetic acid-modified magnetic nanoparticles as a general agent to bind histidine-tagged proteins. J Am Chem Soc, 2004, 126(11): 3392–3393
Robinson A, Fang JM, Chou PT, Liao KW, Chu RM, Lee SJ. Probing lectin and sperm with carbohydrate-modified quantum dots. ChemBioChem, 2005, 6(10): 1899–1905
Nelsestuen GL, Zhang Y, Martinez MB, Key NS, Jilma B, Verneris M, Sinaiko A, Kasthuri RS. Plasma protein profiling: unique and stable features of individuals. Proteomics, 2005, 5(15): 4012–4024
Kreunin P, Yoo C, Urquidi V, Lubman DM, Goodison S. Proteomic profiling identifies breast tumor metastasis-associated factors in an isogenic model. Proteomics, 2007, 7(2): 299–312
Matsui M, Kiyozumi Y, Yamamoto T, Mizushina Y, Mizukami F, Sakaguchi K. Selective adsorption of biopolymers on zeolites. Chem Eur J, 2001, 7(7): 1555–1560
Zhang Y, Wang X, Shan W, Wu B, Fan H, Yu X, Tang Y, Yang P. Enrichment of low-abundance peptides and proteins on zeolite nanocrystals for direct MALDI-TOF MS analysis. Angew Chem Int Ed, 2005, 44(4): 615–617
Daniel MC, Astruc D. Gold nanoparticles: assembly, supramolecular chemistry, quantum-size-related properties, and applications toward biology, catalysis, and nanotechnology. Chem Rev, 2004, 104(1): 293–346
Elghanian R, Storhoff JJ, Mucic RC, Letsinger RL, Mirkin CA. Selective colorimetric detection of polynucleotides based on the distance-dependent optical properties of gold nanoparticles. Science, 1997, 277(5329): 1078–1081
Taton TA, Mirkin CA, Letsinger RL. Scanometric DNA array detection with nanoparticle probes. Science, 2000, 289(5485): 1757–1760
Nam JM, Park SJ, Mirkin CA. Bio-barcodes based on oligonucleotide-modified nanoparticles. J Am Chem Soc, 2002, 124(15): 3820–3821
Teng CH, Ho KC, Lin YS, Chen YC. Gold nanoparticles as selective and concentrating probes for samples in MALDI MS analysis. Anal Chem, 2004, 76(15): 4337–4342
Frens G. Controlled nucleation for the regulation of the particle size in monodisperse gold suspensions. Nat Phys Sci, 1973, 241(105): 20–22
Wang A, Wu CJ, Chen SH. Gold nanoparticle-assisted protein enrichment and electroelution for biological samples containing low protein concentration-a prelude of gel electrophoresis. J Proteome Res, 2006, 5(6): 1488–1492
Sudhir PR, Wu HF, Zhou ZC. Identification of peptides using gold nanoparticle-assisted single-drop microextraction coupled with AP-MALDI mass spectrometry. Anal Chem, 2005, 77(22): 7380–7385
Poh WC, Loh KP. Biosensing properties of diamond and carbon nanotubes. Langmuir, 2004, 20(13): 5484–5492
Chen RJ, Zhang Y, Wang D, Dai H. Noncovalent sidewall functionalization of single-walled carbon nanotubes for protein immobilization. J Am Chem Soc, 2001, 123(16): 3838–3839
Shim M, Kam NWS, Chen RJ, Li Y, Dai H. Functionalization of carbon nanotubes for biocompatibility and biomolecular recognition. Nano Lett, 2002, 2(4): 285–288
Chen WY, Wang LS, Chiu HT, Chen YC, Lee CY. Carbon nanotubes as affinity probes for peptides and proteins in MALDI MS analysis. J Am Soc Mass Spectrom, 2004, 15(11): 1629–1635
Jiang L, Gao L. Modified carbon nanotubes: an effective way to selective attachment of gold nanoparticles. Carbon, 2003, 41(15): 2923–2929
Ren SF, Guo YL. Carbon nanotubes (2,5-dihydroxybenzoyl hydrazine) derivative as pH adjustable enriching reagent and matrix for MALDI analysis of trace peptides. J Am Soc Mass Spectrom, 2006, 17(7): 1023–1027
Pan C, Xu S, Zou H, Guo Z, Zhang Y, Guo B. Carbon nanotubes as adsorbent of solid-phase extraction and matrix for laser desorption/ionization mass spectrometry. J Am Soc Mass Spectrom, 2005, 16(2): 263–270
Li X, Xu S, Pan C, Zhou H, Jiang X, Zhang Y, Ye M, Zou H. Enrichment of peptides from plasma for peptidome analysis using multiwalled carbon nanotubes. J Sep Sci, 2007, 30(6): 930–943
Najam-ul-Haq M, Rainer M, Schwarzenauer T, Huch CW, Bonn GK. Chemically modified carbon nanotubes as material enhanced laser desorption ionisation (MELDI) material in protein profiling. Anal Chim Acta, 2006, 561(1–2): 32–39
Friedman SH, Decamp DL, Sijbesma RP, Srdanov G, Wudl F, Kenyon GL. Inhibition of the HIV-1 protease by fullerene derivatives: model building studies and experimental verification
Shiea J, Huang JP, Teng CF, Jeng J, Wang LY, Chiang LY. Use of a water-soluble fullerene derivative as precipitating reagent and matrix-assisted laser desorption/ionization matrix to selectively detect charged species in aqueous solutions. Anal Chem, 2003, 75(14): 3587–3595
Yu SJ, Kang MW, Chang HC, Chen KM, Yu YC. Bright fluorescent nanodiamonds: no photobleaching and low cytotoxicity. J Am Chem Soc, 2005, 127(50): 17604–17605
Liu KK, Cheng CL, Chang CC, Chao JI. Biocompatible and detectable carboxylated nanodiamond on human cell. Nanotechnology, 2007, 18(32): 325102–325111
Huang LCL, Chang HC. Adsorption and immobilization of cytochrome c on nanodiamonds. Langmuir, 2004, 20(14): 5879–5884
Kong XL, Huang LCL, Hsu CM, Chen WH, Han CC, Chang HC. High-affinity capture of proteins by diamond nanoparticles for mass spectrometric analysis. Anal Chem, 2005, 77(1): 259–265
Chen WH, Lee SC, Sabu S, Fang HC, Chung SC, Han CC, Chang HC. Solid-phase extraction and elution on diamond (SPEED): a fast and general platform for proteome analysis with mass spectrometry. Anal Chem, 2006, 78(12): 4228–4234
Wei LM, Shen Q, Lu HJ, Yang PY. Pretreatment of low-abundance peptides on detonation nanodiamond for direct analysis by matrixassisted laser desorption/ionization time-of-flight mass spectrometry. J Chromatogr B, 2009, 877(29): 3631–3637
Krueger A. New carbon materials: biological applications of functionalized nanodiamond materials. Chem Eur J, 2008, 14(5): 1382–1390
Balazs AC, Emrick T, Russell TP. Nanoparticle polymer composites: where two small worlds meet. Science, 314, 5802: 1107–1110
Jia W, Chen X, Lu H, Yang P. CaCO3-poly(methyl methacrylate) nanoparticles for fast enrichment of low-abundance peptides followed by CaCO3-core removal for MALDI-TOF MS analysis. Angew Chem Int Ed, 2006, 45(20): 3345–3349
Xiong HM, Guan XY, Jin LH, Shen WW, Lu HJ, Xia YY. Surfactant-free synthesis of SnO2@PMMA and TiO2@PMMA core-shell nanobeads designed for peptide/protein enrichment and MALDITOF MS analysis. Angew Chem Int Ed, 2008, 47(22): 4204–4207
Shen W, Xiong H, Xu Y, Cai S, Lu H, Yang P. ZnO-poly(methyl methacrylate) nanobeads for enriching and desalting low-abundant proteins followed by directly MALDI-TOF MS analysis. Anal Chem, 2008, 80(17): 6758–6763
Kresge CT, Leonowics ME, Roth WJ, Vartuli JC, Beck JS. Ordered mesoposous molecular sieves synthesized by a liquid-crystal template mechanism. Nature, 1992, 359(6397): 710–712
Zhao D, Feng J, Huo Q, Melosh N, Fredrickson GH, Chmelka BF, Stucky GD. Triblock copolymer syntheses of mesoporous silica with periodic 50 to 300 angstrom pores. Science, 1998, 279(5350): 548–552
Yang P, Deng T, Zhao D, Feng P, Pine D, Chmelka BF, Whitesides GM, Stucky GD. Hierarchically ordered oxides. Science, 1998, 282(5397): 2244–2246
Yang P, Zhao D, Margolese DI, Chmelka BF, Stucky GD. Generalized syntheses of large-poremesoporous metal oxides with semicrystalline frameworks. Nature, 1998, 396(6707): 152–155
Zuo C, Yu W, Zhou X, Zhao D, Yang P. Highly efficient enrichment and subsequent digestion of proteins in the mesoporous molecular sieve silicate SBA-15 for matrix-assisted laser desorption/ionization mass spectrometry with time-of-flight/time-of-flight analyzer peptide mapping. Rapid Commun Mass Spectrom, 2006(20): 3139–3144
Tian R, Zhang H, Ye M, Jiang X, Hu L, Li X, Bao X, Zou H. Selective extraction of peptides from human plasma by highly ordered mesoporous silica particles for peptidome analysis. Angew Chem Int Ed, 2007, 46(6): 962–965
Tian R, Ye M, Hu L, Li X, Zou H. Selective extraction of peptides in acidic human plasma by porous silica nanoparticles for peptidome analysis with 2-D LC-MS/MS. J Sep Sci, 2007, 30(14): 2204–2209
Tian R, Ren L, Ma H, Li X, Hu L, Ye M, Wu R, Tian Z, Liu Z, Zou H. Selective enrichment of endogenous peptides by chemically modified porous nanoparticles for peptidome analysis. J Chromatogr A, 2009, 1216(8): 1270–1278
Chang SY, Zheng NY, Chen CS, Chen CD, Cheng YY, Wang CRC. Analysis of peptides and proteins affinity-bound to iron oxide nanoparticles by MALDI MS. J Am Soc Mass Spectrom, 2007, 18(5): 910–918
Hunter T. Signaling—2000 and beyond. Cell. 2000, 100(1): 113–127
Kim JK, Mastronardi FG, Wood DD. Lubman DM, Zand R, Moscarello MA. Multiple sclerosis-an important role for post-translational modifications of myelin basic protein in pathogenesis. Mol Cell Proteomics, 2003, 2(7): 453–462
Pandey A, Podtelejnikov AV, Blagoev B, Bustelo XR, Mann M, Lodish HF. Analysis of receptor signaling pathways by mass spectrometry: Identification of Vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors. Proc Natl Acad Sci USA, 2000, 97(1): 179–184
Posewitz MC, Tempst P. Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal Chem, 1999, 71(14): 2883–2892
Pinkse MWH, Uitto PM, Hilhorst MJ, Ooms B, Heck AJR. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal Chem, 2004, 76(14): 3935–3943
Larsen MR, Thingholm TE, Jensen ON, Roepstorff P, Jørgensen TJD. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics, 2005, 4(7): 873–886
Zhou H, Watts JD, Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat Biotechnol, 2001, 19(4): 375–378
Oda Y, Nagasu T, Chait BT. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat Biotechnol, 2001, 19(4): 379–382
Zhang Y, Yu X, Wang X, Shan W, Yang P, Tang Y. Zeolite nanoparticles with immobilized metal ions: isolation and MALDI-TOF-MS/MS identification of phosphopeptides. Chem Commun, 2004, 24: 2882–2883
Pan C, Ye M, Liu Y, Feng S, Jiang X, Han G, Zhu J, Zou H. Enrichment of phosphopeptides by Fe3+-immobilized mesoporous nanoparticles of MCM-41 for MALDI and nano-LC-MS/MS analysis. J Proteome Res, 2006, 5(11): 3114–3124
Hu L, Zhou H, Li Y, Sun S, Guo L, Ye M, Tian X, Gu J, Yang S, Zou H. Profiling of endogenous serum phosphorylated peptides by titanium (IV) immobilized mesoporous silica particles enrichment and MALDI-TOFMS detection. Anal Chem, 2009, 81(1): 94–104
Tan F, Zhang Y, Mi W, Wang J, Wei J, Cai Y, Qian X. Enrichment of phosphopeptides by Fe3+-immobilized magnetic nanoparticles for phosphoproteome analysis of the plasma membrane of mouse liver. J Proteome Res, 2008, 7(3): 1078–1087
Zhou H, Tian R, Ye M, Xu S, Feng S, Pan C, Jiang X, Li X, Zou H. Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis. Electrophoresis, 2007, 28(13): 2201–2215
Nelson CA, Szczech JR, Xu Q, Lawrence MJ, Jin S, Ge Y. Mesoporous zirconium oxide nanomaterials effectively enrich phosphopeptides for mass spectrometry-based phosphoproteomics. Chem Commun, 2009, 43: 6607–6609
Liang SS, Makamba H, Huang SY, Chen SH. Nano-titanium dioxide composites for the enrichment of phosphopeptides. J Chromatogr A, 2006, 1116(1–2): 38–45
Hsieh HC, Sheu C, Shi FK, Li DT. Development of a titanium dioxide nanoparticle pipette-tip for the selective enrichment of phosphorylated peptides. J Chromatogr A, 2007, 1165(1–2): 128–135
Chen CT, Chen YC. Fe3O4/TiO2 core/shell nanoparticles as affinity probes for the analysis of phosphopeptides using TiO2 surface-assisted laser desorption/ionization mass spectrometry. Anal Chem, 2005, 77(18): 5912–5919
Chen CT, Chen YC. A two-matrix system for MALDI MS analysis of serine phosphorylated peptides concentrated by Fe3O4/Al2O3 magnetic nanoparticles. J Mass Spectrom, 2008, 43(4): 538–541
Lin HY, Chen WY, Chen YC. Iron oxide/tantalum oxide core-shell magnetic nanoparticle-based microwave-assisted extraction for phosphopeptide enrichment from complex samples for MALDI MS analysis. Anal Bioanal Chem, 2009, 394(8): 2129–2136
Qiao L, Roussel C, Wan J, Yang P, Girault HH, Liu B. Specific on-plate enrichment of phosphorylated peptides for direct MALDI-TOF MS analysis. J Proteome Res, 2007, 6(12): 4763–4769
Tian Y, Zhou Y, Elliott S, Aebersold R, Zhang H. Solid-phase extraction of N-linked glycopeptides. Nat Protoc, 2007, 2(2): 334–339
Wu L, Han DK. Overcoming the dynamic range problem in mass spectrometry-based shotgun proteomics. Expert Rev Proteomics, 2006, 3(6): 611–619
Zhang L, Lu H, Yang P. Specific enrichment methods for glycoproteome research. Anal Bioanal Chem, 2010, 396(1): 199–203
Yeap WS, Tan YY, Loh KP. Using detonation nanodiamond for the specific capture of glycoproteins. Anal Chem, 2008, 80(12): 4659–4665
Zhou W, Yao N, Yao G, Deng C, Zhang X, Yang P. Facile synthesis of aminophenylboronic acid-functionalized magnetic nanoparticles for selective separation of glycopeptides and glycoproteins. Chem Commun, 2008, 43: 5577–5579
Xu Y, Wu X, Zhang L, Lu H, Yang P, Webley PA, Zhao D. Highly specific enrichment of glycopeptides using boronic acid-functionalized mesoporous silica. Anal Chem, 2009, 81(1): 503–508
Zhang L, Xu Y, Yao H, Xie L, Yao J, Lu H, Yang P. Boronic acid functionalized core-satellite composite nanoparticles for advanced enrichment of glycopeptides and glycoproteins. Chem Eur J, 2009, 15(39): 10158–10166
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Support from the Major State Basie Research Development Program (Grant No. 2007CB914100), the National Natural Science Foundation of China (Grant Nos. 20875016 & 20735005), the Ph.D. Programs Foundation of the Ministry of Education of China (Grant No. 200802460011), and Shanghai Projects (Grant Nos. 08DZ2293601, Eastern Scholar, Shu Guang and B109).
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Zhang, L., Lu, H. & Yang, P. Recent developments of nanoparticle-based enrichment methods for mass spectrometric analysis in proteomics. Sci. China Chem. 53, 695–703 (2010). https://doi.org/10.1007/s11426-010-0112-1
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DOI: https://doi.org/10.1007/s11426-010-0112-1