Abstract
Intracellular delivery of functional proteins using nanoparticles can be a game-changing approach for cancer therapy. However, cytosolic release of functional protein is still a major challenge. In addition, formation of protein corona on the surface of the nanoparticles can also alter the behavior of the nanoparticles. Here, we will review recent strategies for protein delivery into the cell. Finally we will discuss the issue of protein corona formation in light of nanoparticle-protein interactions.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Foster S, Duvall CL, Crownover EF, Hoffman AS, Stayton PS (2010) Intracellular delivery of a protein antigen with an endosomal-releasing polymer enhances CD8 T-cell production and prophylactic vaccine efficacy. Bioconjug Chem 21(12):2205–2212
Vasconcelos L, Pärn K, Langel Ü (2013) Therapeutic potential of cell-penetrating peptides. Ther Deliv 4(5):573–591
Kratz F, Elsadek B (2012) Clinical impact of serum proteins on drug delivery. J Controlled Release 161(2):429–445
Le Roy C, Wrana JL (2005) Clathrin-and non-clathrin-mediated endocytic regulation of cell signalling. Nat Rev Mol Cell Biol 6(2):112–126
Mellert K, Lamla M, Scheffzek K, Wittig R, Kaufmann D (2012) Enhancing endosomal escape of transduced proteins by photochemical internalisation. PLoS ONE 7(12):e52473
Yan B, Kim ST, Kim CS, Saha K, Moyano DF, Xing Y, Jiang Y, Roberts AL, Alfonso FS, Rotello VM, Vachet RW (2013) Multiplexed Imaging of Nanoparticles in Tissues Using Laser Desorption/Ionization Mass Spectrometry. J Am Chem Soc 135(34):12564–12567. doi:10.1021/ja406553f
Tang R, Kim CS, Solfiell DJ, Rana S, Mout R, Velázquez-Delgado EM, Chompoosor A, Jeong Y, Yan B, Zhu Z-J, Kim C, Hardy JA, Rotello VM (2013) Direct delivery of functional proteins and enzymes to the cytosol using nanoparticle-stabilized nanocapsules. ACS Nano 7(8):6667–6673. doi:10.1021/nn402753y
De M, Rana S, Akpinar H, Miranda OR, Arvizo RR, Bunz UHF, Rotello VM (2009) Sensing of proteins in human serum using conjugates of nanoparticles and green fluorescent protein. Nat Chem 1(6):461–465. doi:10.1038/nchem.334
Saha K, Agasti SS, Kim C, Li X, Rotello VM (2012) Gold nanoparticles in chemical and biological sensing. Chem Rev 112(5):2739–2779. doi:10.1021/cr2001178
Yang S-T, Liu Y, Wang Y-W, Cao A (2013) Biosafety and bioapplication of nanomaterials by designing protein-nanoparticle interactions. Small 9(9–10):1635–1653. doi:10.1002/smll.201201492
De M, Miranda OR, Rana S, Rotello VM (2009) Size and geometry dependent protein-nanoparticle self-assembly. Chem Commun 16:2157–2159. doi:10.1039/b900552h
You CC, Agasti SS, De M, Knapp MJ, Rotello VM (2006) Modulation of the catalytic behavior of α-chymotrypsin at monolayer-protected nanoparticle surfaces. J Am Chem Soc 128(45):14612–14618. doi:10.1021/ja064433z
You CC, De M, Rotello VM (2005) Contrasting effects of exterior and interior hydrophobic moieties in the complexation of amino acid functionalized gold clusters with α-chymotrypsin. Org Lett 7(25):5685–5688. doi:10.1021/ol052367k
You CC, De M, Han G, Rotello VM (2005) Tunable inhibition and denaturation of α-chymotrypsin with amino acid-functionalized gold nanoparticles. J Am Chem Soc 127(37):12873–12881. doi:10.1021/ja0512881
De M, Rotello VM (2008) Synthetic “chaperones”: nanoparticle-mediated refolding of thermally denatured proteins. Chem Commun 30:3504–3506. doi:10.1039/b805242e
Kim M-S, Pinto SM, Getnet D, Nirujogi RS, Manda SS, Chaerkady R, Madugundu AK, Kelkar DS, Isserlin R, Jain S (2014) A draft map of the human proteome. Nature 509(7502):575–581
Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333–366
Laurent S, Saei AA, Behzadi S, Panahifar A, Mahmoudi M (2014) Superparamagnetic iron oxide nanoparticles for delivery of therapeutic agents: opportunities and challenges. Expert Opin Drug Deliv 0:1–22
Zhang Y, Meibohm B (2012) Pharmacokinetics and pharmacodynamics of therapeutic peptides and proteins. In: Pharmaceutical biotechnology: drug discovery and clinical applications, 2nd edn. Wiley, Weinheim, pp 337–367
Molema G, de Leij LF, Meijer DK (1997) Tumor vascular endothelium: barrier or target in tumor directed drug delivery and immunotherapy. Pharm Res 14(1):2–10
Netti PA, Berk DA, Swartz MA, Grodzinsky AJ, Jain RK (2000) Role of extracellular matrix assembly in interstitial transport in solid tumors. Cancer Res 60(9):2497–2503
Matsumura Y, Maeda H (1986) A new concept for macromolecular therapeutics in cancer-chemotherapy—mechanism of tumoritropic accumulation of proteins and the antitumor agent Smancs. Cancer Res 46(12):6387–6392
Dexter DL, Kowalski HM, Blazar BA, Fligiel Z, Vogel R, Heppner GH (1978) Heterogeneity of tumor cells from a single mouse mammary tumor. Cancer Res 38(10):3174–3181
Cheever MA, Higano CS (2011) Provenge (Sipuleucel-T) in prostate cancer: the first FDA-approved therapeutic cancer vaccine. Clin Cancer Res 17(11):3520–3526
Ghosh P, Yang X, Arvizo R, Zhu Z-J, Agasti SS, Mo Z, Rotello VM (2010) Intracellular delivery of a membrane-impermeable enzyme in active form using functionalized gold nanoparticles. J Am Chem Soc 132(8):2642–2645
Yan M, Du J, Gu Z, Liang M, Hu Y, Zhang W, Priceman S, Wu L, Zhou ZH, Liu Z (2009) A novel intracellular protein delivery platform based on single-protein nanocapsules. Nat Nanotechnol 5(1):48–53
Folkes LK, Wardman P (2001) Oxidative activation of indole-3-acetic acids to cytotoxic species—a potential new role for plant auxins in cancer therapy. Biochem Pharmacol 61(2):129–136
de Melo MP, de Lima TM, Pithon-Curi TC, Curi R (2004) The mechanism of indole acetic acid cytotoxicity. Toxicol Lett 148(1):103–111
Yeh YC, Tang R, Mout R, Jeong Y, Rotello VM (2014) Fabrication of multiresponsive bioactive nanocapsules through orthogonal self-assembly. Angew Chem Int Edit 53(20):5137–5141
Allen TM, Cullis PR (2013) Liposomal drug delivery systems: from concept to clinical applications. Adv Drug Deliver Rev 65 (1):36–48. doi:http://dx.doi.org/10.1016/j.addr.2012.09.037
Anderson PM, Hanson DC, Hasz DE, Halet MR, Blazar BR, Ochoa AC (1994) Cytokines in liposomes: preliminary studies with IL-1, IL-2, IL-6. GM-CSF and interferon-γ. Cytokine 6(1):92–101
Meyer J, Whitcomb L, Collins D (1994) Efficient encapsulation of proteins within liposomes for slow release in vivo. Biochem Biophys Res Commun 199(2):433–438
Ye Q, Asherman J, Stevenson M, Brownson E, Katre NV (2000) DepoFoam™ technology: a vehicle for controlled delivery of protein and peptide drugs. J Controlled Release 64(1):155–166
Liguori L, Marques B, Villegas-Mendez A, Rothe R, Lenormand J-L (2008) Liposomes-mediated delivery of pro-apoptotic therapeutic membrane proteins. J Controlled Release 126(3):217–227
Gao J, Zhong W, He J, Li H, Zhang H, Zhou G, Li B, Lu Y, Zou H, Kou G (2009) Tumor-targeted PE38KDEL delivery via PEGylated anti-HER2 immunoliposomes. Int J Pharm 374(1):145–152
Yoshikawa T, Okada N, Oda A, Matsuo K, Matsuo K, Mukai Y, Yoshioka Y, Akagi T, Akashi M, Nakagawa S (2008) Development of amphiphilic γ-PGA-nanoparticle based tumor vaccine: potential of the nanoparticulate cytosolic protein delivery carrier. Biochem Biophys Res Commun 366(2):408–413
Bramwell VW, Eyles JE, Oya Alpar H (2005) Particulate delivery systems for biodefense subunit vaccines. Adv Drug Deliver Rev 57(9):1247–1265
Kaczmarczyk SJ, Sitaraman K, Young HA, Hughes SH, Chatterjee DK (2011) Protein delivery using engineered virus-like particles. Proc Natl Acad Sci USA 108(41):16998–17003
Harris JM, Chess RB (2003) Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov 2(3):214–221
Torchilin VP, Lukyanov AN (2003) Peptide and protein drug delivery to and into tumors: challenges and solutions. Drug Discov Today 8(6):259–266
Carswell E, Old LJ, Kassel R, Green S, Fiore N, Williamson B (1975) An endotoxin-induced serum factor that causes necrosis of tumors. Proc Natl Acad Sci USA 72(9):3666–3670
Lejeune F (1995) High dose recombinant tumour necrosis factor (rTNFα) administered by isolation perfusion for advanced tumours of the limbs: a model for biochemotherapy of cancer. Eur J Cancer 31(6):1009–1016
Liénard D, Lejeune FJ, Ewalenko P (1992) In transit metastases of malignant melanoma treated by high dose rTNFα in combination with interferon-γ and melphalan in isolation perfusion. World J Surg 16(2):234–240
Paciotti GF, Myer L, Weinreich D, Goia D, Pavel N, McLaughlin RE, Tamarkin L (2004) Colloidal gold: a novel nanoparticle vector for tumor directed drug delivery. Drug Deliv 11(3):169–183
Paciotti GF, Kingston DG, Tamarkin L (2006) Colloidal gold nanoparticles: a novel nanoparticle platform for developing multifunctional tumor-targeted drug delivery vectors. Drug Develop Res 67(1):47–54
Libutti S, Paciotti G, Myer L, Haynes R, Gannon W, Walker M, Seidel G, Byrnes A, Yuldasheva N, Tamarkin L (2009) Results of a completed phase I clinical trial of CYT-6091: A pegylated colloidal gold-TNF nanomedicine. J Clin Oncol (Meeting Abstracts) 15S:3586
Brinãs RP, Sundgren A, Sahoo P, Morey S, Rittenhouse-Olson K, Wilding GE, Deng W, Barchi Jr JJ (2012) Design and synthesis of multifunctional gold nanoparticles bearing tumor-associated glycopeptide antigens as potential cancer vaccines. Bioconjug Chem 23(8):1513–1523
Mandal M, Lee K-D (2002) Listeriolysin O-liposome-mediated cytosolic delivery of macromolecule antigen in vivo: enhancement of antigen-specific cytotoxic T lymphocyte frequency, activity, and tumor protection. BBA-Biomembr 1563(1):7–17
Provoda CJ, Stier EM, Lee K-D (2003) Tumor cell killing enabled by listeriolysin O-liposome-mediated delivery of the protein toxin gelonin. J Biol Chem 278(37):35102–35108
Gaspar M, Perez-Soler R, Cruz M (1996) Biological characterization of L-asparaginase liposomal formulations. Cancer Chemother Pharmacol 38(4):373–377
Jorge JC, Perez-Soler R, Morais JG, Cruz MEM (1994) Liposomal palmitoyl-L-asparaginase: characterization and biological activity. Cancer Chemoth Pharm 34(3):230–234
Kanaoka E, Takahashi K, Yoshikawa T, Jizomoto H, Nishihara Y, Uchida N, Maekawa R, Hirano K (2002) A significant enhancement of therapeutic effect against hepatic metastases of M5076 in mice by a liposomal interleukin-2 (mixture). J Controlled Release 82(2):183–187
Wakita D, Chamoto K, Zhang Y, Narita Y, Noguchi D, Ohnishi H, Iguchi T, Sakai T, Ikeda H, Nishimura T (2006) An indispensable role of type-1 IFNs for inducing CTL-mediated complete eradication of established tumor tissue by CpG-liposome co-encapsulated with model tumor antigen. Int Immunol 18(3):425–434
Daftarian P, Mansour M, Benoit AC, Pohajdak B, Hoskin DW, Brown RG, Kast WM (2006) Eradication of established HPV 16-expressing tumors by a single administration of a vaccine composed of a liposome-encapsulated CTL-T helper fusion peptide in a water-in-oil emulsion. Vaccine 24(24):5235–5244
Kwak LW, Pennington R, Boni L, Ochoa AC, Robb RJ, Popescu MC (1998) Cutting edge: liposomal formulation of a self lymphoma antigen induces potent protective antitumor immunity. J Immunol 160(8):3637–3641
Neelapu SS, Baskar S, Gause BL, Kobrin CB, Watson TM, Frye AR, Pennington R, Harvey L, Jaffe ES, Robb RJ (2004) Human autologous tumor-specific T-cell responses induced by liposomal delivery of a lymphoma antigen. Clin Cancer Res 10(24):8309–8317
Kim J-H, Kim Y-S, Park K, Kang E, Lee S, Nam HY, Kim K, Park JH, Chi DY, Park R-W (2008) Self-assembled glycol chitosan nanoparticles for the sustained and prolonged delivery of antiangiogenic small peptide drugs in cancer therapy. Biomaterials 29(12):1920–1930
Lim SM, Kim TH, Jiang HH, Park CW, Lee S, Chen X, Lee KC (2011) Improved biological half-life and anti-tumor activity of TNF-related apoptosis-inducing ligand (TRAIL) using PEG-exposed nanoparticles. Biomaterials 32(13):3538–3546
Gao J, Kou G, Chen H, Wang H, Li B, Lu Y, Zhang D, Wang S, Hou S, Qian W (2008) Treatment of hepatocellular carcinoma in mice with PE38KDEL type I mutant-loaded poly (lactic-co-glycolic acid) nanoparticles conjugated with humanized SM5-1 F (ab′) fragments. Mol Cancer Ther 7(10):3399–3407
Li YP, Pei YY, Zhou ZH, Zhang XY, Gu ZH, Ding J, Zhou JJ, Gao XJ, Zhu JH (2001) Stealth polycyanoacrylate nanoparticles as tumor necrosis factor-ALPHA. Carriers: pharmacokinetics and anti-tumor effects. Biol Pharm Bull 24(6):662–665
Tenzer S, Docter D, Kuharev J, Musyanovych A, Fetz V, Hecht R, Schlenk F, Fischer D, Kiouptsi K, Reinhardt C (2013) Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology. Nat Nanotechnol 8(10):772–781
Gagner JE, Lopez MD, Dordick JS, Siegel RW (2011) Effect of gold nanoparticle morphology on adsorbed protein structure and function. Biomaterials 32(29):7241–7252
Mahmoudi M, Shokrgozar MA, Behzadi S (2013) Slight temperature changes affect protein affinity and cellular uptake/toxicity of nanoparticles. Nanoscale 5(8):3240–3244
Mahmoudi M, Serpooshan V (2011) Large protein absorptions from small changes on the surface of nanoparticles. J Phys Chem C 115(37):18275–18283
Cedervall T, Lynch I, Foy M, Berggård T, Donnelly SC, Cagney G, Linse S, Dawson KA (2007) Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew Chem Int Ed 46(30):5754–5756
Yeh Y-C, Rana S, Mout R, Yan B, Alfonso FS, Rotello VM (2014) Supramolecular tailoring of protein–nanoparticle interactions using cucurbituril mediators. Chem Commun 50(42):5565–5568
Zhu ZJ, Posati T, Moyano DF, Tang R, Yan B, Vachet RW, Rotello VM (2012) The interplay of monolayer structure and serum protein interactions on the cellular uptake of gold nanoparticles. Small 8(17):2659–2663
Mahmoudi M, Abdelmonem AM, Behzadi S, Clement JH, Dutz S, Ejtehadi MR, Hartmann R, Kantner K, Linne U, Maffre P (2013) Temperature: the “ignored” factor at the nanobio interface. ACS Nano 7(8):6555–6562
Maiorano G, Sabella S, Sorce B, Brunetti V, Malvindi MA, Cingolani R, Pompa PP (2010) Effects of cell culture media on the dynamic formation of protein—nanoparticle complexes and influence on the cellular response. ACS Nano 4(12):7481–7491
Laurent S, Burtea C, Thirifays C, Rezaee F, Mahmoudi M (2013) Significance of cell “observer” and protein source in nanobiosciences. J Colloid Interface Sci 392:431–445
Casals E, Pfaller T, Duschl A, Oostingh GJ, Puntes V (2010) Time evolution of the nanoparticle protein corona. ACS Nano 4(7):3623–3632
Monopoli MP, Walczyk D, Campbell A, Elia G, Lynch I, Baldelli Bombelli F, Dawson KA (2011) Physical—chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles. J Am Chem Soc 133(8):2525–2534
Caracciolo G, Pozzi D, Capriotti AL, Cavaliere C, Foglia P, Amenitsch H, Laganà A (2011) Evolution of the protein corona of lipid gene vectors as a function of plasma concentration. Langmuir 27(24):15048–15053
Ghavami M, Saffar S, Emamy BA, Peirovi A, Shokrgozar MA, Serpooshan V, Mahmoudi M (2013) Plasma concentration gradient influences the protein corona decoration on nanoparticles. RSC Adv 3(4):1119–1126
Nakanishi K, Sakiyama T, Imamura K (2001) On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon. J Biosci Bioeng 91(3):233–244
Gessner A, Lieske A, Paulke BR, Müller RH (2003) Functional groups on polystyrene model nanoparticles: influence on protein adsorption. J Biomed Mater Res, Part A 65(3):319–326
Choi CHJ, Hao L, Narayan SP, Auyeung E, Mirkin CA (2013) Mechanism for the endocytosis of spherical nucleic acid nanoparticle conjugates. Proc Natl Acad Sci USA 110(19):7625–7630
Mahmoudi M, Lynch I, Ejtehadi MR, Monopoli MP, Bombelli FB, Laurent S (2011) Protein-nanoparticle interactions: opportunities and challenges. Chem Rev 111(9):5610–5637
Lundqvist M, Stigler J, Elia G, Lynch I, Cedervall T, Dawson KA (2008) Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc Natl Acad Sci USA 105(38):14265–14270
Vroman L (1962) Effect of Adsorbed Proteins on the Wettability of Hydrophilic and Hydrophobic Solids. Nature 196(4853):476–477
Hajipour MJ, Laurent S, Aghaie A, Rezaee F, Mahmoudi M (2014) Personalized protein coronas: a “key” factor at the nanobiointerface. Biomater Sci 2(9):1210–1221. doi:10.1039/c4bm00131a
Nagayama S, K-i Ogawara, Fukuoka Y, Higaki K, Kimura T (2007) Time-dependent changes in opsonin amount associated on nanoparticles alter their hepatic uptake characteristics. Int J Pharm 342(1):215–221
Lunov O, Syrovets T, Loos C, Beil J, Delacher M, Tron K, Nienhaus GU, Musyanovych A, Mailander V, Landfester K (2011) Differential uptake of functionalized polystyrene nanoparticles by human macrophages and a monocytic cell line. ACS Nano 5(3):1657–1669
Kobzik L (1995) Lung macrophage uptake of unopsonized environmental particulates role of scavenger-type receptors. J Immunol 155(1):367–376
Hamilton RF, Thakur SA, Mayfair JK, Holian A (2006) MARCO mediates silica uptake and toxicity in alveolar macrophages from C57BL/6 mice. J Biol Chem 281(45):34218–34226
Walkey CD, Olsen JB, Guo H, Emili A, Chan WC (2012) Nanoparticle size and surface chemistry determine serum protein adsorption and macrophage uptake. J Am Chem Soc 134(4):2139–2147
Deng ZJ, Liang M, Monteiro M, Toth I, Minchin RF (2011) Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation. Nat Nanotechnol 6(1):39–44
Decuzzi P, Godin B, Tanaka T, Lee S-Y, Chiappini C, Liu X, Ferrari M (2010) Size and shape effects in the biodistribution of intravascularly injected particles. J Controlled Release 141(3):320–327
Hamad I, Al-Hanbali O, Hunter AC, Rutt KJ, Andresen TL, Moghimi SM (2010) Distinct polymer architecture mediates switching of complement activation pathways at the nanosphere – serum interface: implications for stealth nanoparticle engineering. ACS Nano 4(11):6629–6638
Rubel C, Fernández GC, Dran G, Bompadre MB, Isturiz MA, Palermo MS (2001) Fibrinogen promotes neutrophil activation and delays apoptosis. J Immunol 166(3):2002–2010
Sitrin RG, Pan PM, Srikanth S, Todd RF (1998) Fibrinogen activates NF-κB transcription factors in mononuclear phagocytes. J Immunol 161(3):1462–1470
McNally A, Anderson J (1994) Complement C3 participation in monocyte adhesion to different surfaces. Proc Natl Acad Sci USA 91(21):10119–10123
Tandia B-M, Vandenbranden M, Wattiez R, Lakhdar Z, Ruysschaert J-M, Elouahabi A (2003) Identification of human plasma proteins that bind to cationic lipid/DNA complex and analysis of their effects on transfection efficiency: implications for intravenous gene transfer. Mol Ther 8(2):264–273
Paula AJ, Araujo Júnior RT, Martinez DST, Paredes-Gamero EJ, Nader HB, Durán N, Justo GZ, Alves OL (2013) Influence of protein corona on the transport of molecules into cells by mesoporous silica nanoparticles. ACS Appl Mater Inter 5(17):8387–8393
Lesniak A, Fenaroli F, Monopoli MP, Åberg C, Dawson KA, Salvati A (2012) Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells. ACS Nano 6(7):5845–5857
Jiang X, Weise S, Hafner M, Röcker C, Zhang F, Parak WJ, Nienhaus GU (2009) Quantitative analysis of the protein corona on FePt nanoparticles formed by transferrin binding. J R Soc Interface. doi:10.1098/rsif.2009.0272.focus
Zhu Y, Li W, Li Q, Li Y, Li Y, Zhang X, Huang Q (2009) Effects of serum proteins on intracellular uptake and cytotoxicity of carbon nanoparticles. Carbon 47(5):1351–1358
JosepháJerry D (2009) Stability, toxicity and differential cellular uptake of protein passivated-Fe3O4 nanoparticles. J Mater Chem 19(35):6328–6331
Guarnieri D, Guaccio A, Fusco S, Netti PA (2011) Effect of serum proteins on polystyrene nanoparticle uptake and intracellular trafficking in endothelial cells. J Nanopart Res 13(9):4295–4309
Ruge CA, Kirch J, Cañadas O, Schneider M, Perez-Gil J, Schaefer UF, Casals C, Lehr C-M (2011) Uptake of nanoparticles by alveolar macrophages is triggered by surfactant protein A. Nanomed-Nanotechnol 7(6):690–693
Wang Z, Tiruppathi C, Minshall RD, Malik AB (2009) Size and dynamics of caveolae studied using nanoparticles in living endothelial cells. ACS Nano 3(12):4110–4116
Caracciolo G, Callipo L, De Sanctis SC, Cavaliere C, Pozzi D, Laganà A (2010) Surface adsorption of protein corona controls the cell internalization mechanism of DC-Chol–DOPE/DNA lipoplexes in serum. BBA-Biomembr 1798(3):536–543
Pitek AS, O’Connell D, Mahon E, Monopoli MP, Bombelli FB, Dawson KA (2012) Transferrin coated nanoparticles: study of the bionano interface in human plasma. PLoS ONE 7(7):e40685
Salvati A, Pitek AS, Monopoli MP, Prapainop K, Bombelli FB, Hristov DR, Kelly PM, Åberg C, Mahon E, Dawson KA (2013) Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule corona adsorbs on the surface. Nat Nanotechnol 8(2):137–143
Mirshafiee V, Mahmoudi M, Lou K, Cheng J, Kraft ML (2013) Protein corona significantly reduces active targeting yield. Chem Commun 49(25):2557–2559
Mahon E, Salvati A, Baldelli Bombelli F, Lynch I, Dawson KA (2012) Designing the nanoparticle–biomolecule interface for “targeting and therapeutic delivery”. J Controlled Release 161(2):164–174
Caracciolo G (2012) The protein corona effect for targeted drug delivery. Bioinspired Biomimetic Nanobiomaterials 2(1):54–57
Moyano DF, Saha K, Prakash G, Yan B, Kong H, Yazdani M, Rotello VM (2014) Fabrication of corona-free nanoparticles with tunable hydrophobicity. ACS Nano 8(7):6748–6755. doi:10.1021/nn5006478
Kah JCY, Chen J, Zubieta A, Hamad-Schifferli K (2012) Exploiting the protein corona around gold nanorods for loading and triggered release. ACS Nano 6(8):6730–6740
Cifuentes-Rius A, de Puig H, Kah JCY, Borros S, Hamad-Schifferli K (2013) Optimizing the properties of the protein corona surrounding nanoparticles for tuning payload release. ACS Nano 7(11):10066–10074
Högemann-Savellano D, Bos E, Blondet C, Sato F, Abe T, Josephson L, Weissleder R, Gaudet J, Sgroi D, Peters PJ (2003) The transferrin receptor: a potential molecular imaging marker for human cancer. Neoplasia (New York, NY) 5(6):495
Daniels TR, Delgado T, Helguera G, Penichet ML (2006) The transferrin receptor part II: targeted delivery of therapeutic agents into cancer cells. Clin Immunol 121(2):159–176
Berggård T, Arrigoni G, Olsson O, Fex M, Linse S, James P (2006) 140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry. J Proteome Res 5(3):669–687
Labarre D, Vauthier C, Chauvierre C, Petri B, Müller R, Chehimi MM (2005) Interactions of blood proteins with poly (isobutylcyanoacrylate) nanoparticles decorated with a polysaccharidic brush. Biomaterials 26(24):5075–5084
Cushley RJ, Okon M (2002) NMR studies of lipoprotein structure. Annu Rev Biophys Biomol Struct 31(1):177–206
Srivastava RAK (2003) Scavenger receptor class B type I expression in murine brain and regulation by estrogen and dietary cholesterol. J Neurol Sci 210(1):11–18
Goti D, Hrzenjak A, Levak-Frank S, Frank S, Van Der Westhuyzen DR, Malle E, Sattler W (2001) Scavenger receptor class B, type I is expressed in porcine brain capillary endothelial cells and contributes to selective uptake of HDL-associated vitamin E. J Neurochem 76(2):498–508
Panzenboeck U, Balazs Z, Sovic A, Hrzenjak A, Levak-Frank S, Wintersperger A, Malle E, Sattler W (2002) ABCA1 and scavenger receptor class B, type I, are modulators of reverse sterol transport at an in vitro blood-brain barrier constituted of porcine brain capillary endothelial cells. J Biol Chem 277(45):42781–42789
Zannis VI, Chroni A, Krieger M (2006) Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL. J Mol Med 84(4):276–294
Hammad SM, Stefansson S, Twal WO, Drake CJ, Fleming P, Remaley A, Brewer HB, Argraves WS (1999) Cubilin, the endocytic receptor for intrinsic factor-vitamin B12 complex, mediates high-density lipoprotein holoparticle endocytosis. Proc Natl Acad Sci USA 96(18):10158–10163
Kozyraki R, Fyfe J, Kristiansen M, Gerdes C, Jacobsen C, Cui S, Christensen EI, Aminoff M, de la Chapelle A, Krahe R (1999) The intrinsic factor–vitamin B12 receptor, cubilin, is a high-affinity apolipoprotein AI receptor facilitating endocytosis of high-density lipoprotein. Nat Med 5(6):656–661
Sahali D, Mulliez N, Chatelet F, Dupuis R, Ronco P, Verroust P (1988) Characterization of a 280-kD protein restricted to the coated pits of the renal brush border and the epithelial cells of the yolk sac. Teratogenic effect of the specific monoclonal antibodies. J Exp Med 167(1):213–218
Seetharam B, Christensen EI, Moestrup SK, Hammond TG, Verroust PJ (1997) Identification of rat yolk sac target protein of teratogenic antibodies, gp280, as intrinsic factor-cobalamin receptor. J Clin Investig 99(10):2317
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2015 Springer International Publishing Switzerland
About this chapter
Cite this chapter
Saie, A.A., Ray, M., Mahmoudi, M., Rotello, V.M. (2015). Engineering the Nanoparticle-Protein Interface for Cancer Therapeutics. In: Mirkin, C., Meade, T., Petrosko, S., Stegh, A. (eds) Nanotechnology-Based Precision Tools for the Detection and Treatment of Cancer. Cancer Treatment and Research, vol 166. Springer, Cham. https://doi.org/10.1007/978-3-319-16555-4_11
Download citation
DOI: https://doi.org/10.1007/978-3-319-16555-4_11
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-16554-7
Online ISBN: 978-3-319-16555-4
eBook Packages: MedicineMedicine (R0)