Protein–Nanoparticle Interaction: Corona Formation and Conformational Changes in Proteins on Nanoparticles

References

• Monopoli MP, Aberg C, Salvati A, Dawson KA. Biomolecular coronas provide the biological identity of nanosized materials. Nat Nanotechnol. 2012;7(12):779–786. doi:10.1038/nnano.2012.20723212421
   PubMed Web of Science ®Google Scholar
• Sun T, Zhang YS, Pang B, Hyun DC, Yang M, Xia Y. Engineered nanoparticles for drug delivery in cancer therapy. Angew Chem Int Ed. 2014;53:12320–12364.
   PubMed Web of Science ®Google Scholar
• Anselmo AC, Mitragotri S. Nanoparticles in the clinic. Bioeng Transl Med. 2016;1:10–29.29313004
   PubMed Web of Science ®Google Scholar
• Bobo D, Robinson KJ, Islam J, et al. Nanoparticle-based medicines: a review of FDA-approved materials and clinical trials to date. Pharm Res. 2016;33(10):2373–2387. doi:10.1007/s11095-016-1958-527299311
   PubMed Web of Science ®Google Scholar
• Papi M, Caputo D, Palmieri V, et al. Clinically approved PEGylated nanoparticles are covered by a protein corona that boosts the uptake by cancer cells. Nanoscale. 2017;9:10327–10334. doi:10.1039/C7NR03042H28702661
   PubMed Web of Science ®Google Scholar
• Guttmann A, Krasnokutsky S, Pillinger MH, Berhanu A. Pegloticase in gout treatment—safety issues, latest evidence and clinical considerations. Ther Adv Drug Saf. 2017;8:379–388. doi:10.1177/204209861772771429204266
   PubMed Web of Science ®Google Scholar
• English C, Aloi JJ. New FDA-approved disease-modifying therapies for multiple sclerosis. Clin Ther. 2015;37:691–715. doi:10.1016/j.clinthera.2015.03.00125846320
   PubMed Web of Science ®Google Scholar
• Edgar JYC, Wang H. Introduction for design of nanoparticle based drug delivery systems. Curr Pharm Des. 2017;23(14):2108–2112. doi:10.2174/138161282266616102515400327784242
   PubMed Web of Science ®Google Scholar
• Matoba T, Koga JI, Nakano K, Egashira K, Tsutsui H. Nanoparticle-mediated drug delivery system for atherosclerotic cardiovascular disease. J Cardiol. 2017;70(3):206–211. doi:10.1016/j.jjcc.2017.03.00528416142
   PubMed Web of Science ®Google Scholar
• Mishra D, Hubenak JR, Mathur AB. Nanoparticle systems as tools to improve drug delivery and therapeutic efficacy. J Biomed Mater Res A. 2013;101(12):3646–3660. doi:10.1002/jbm.a.3464223878102
   PubMed Web of Science ®Google Scholar
• Conte R, Marturano V, Peluso G, Calarco A, Cerruti P. Recent advances in nanoparticle-mediated delivery of anti-inflammatory phytocompounds. Int J Mol Sci. 2017;18(4):709. doi:10.3390/ijms18040709
   PubMed Web of Science ®Google Scholar
• Lin YS, Lee MY, Yang CH, Huang KS. Active targeted drug delivery for microbes using nano-carriers. Curr Top Med Chem. 2015;15(15):1525–1531. doi:10.2174/156802661566615041412315725877093
   PubMed Web of Science ®Google Scholar
• Yeon Kyung L, Eun-Ju C, Thomas JW, Sang-Hyun K, Dongwoo K. Effect of the protein corona on nanoparticles for modulating cytotoxicity and immunotoxicity. Int J Nanomedicine. 2015;10:97–113. doi:10.2147/IJN.S7299825565807
   PubMed Web of Science ®Google Scholar
• Szebeni J, Simberg D, González-Fernández Á, Barenholz Y, Dobrovolskaia MA. Roadmap and strategy for overcoming infusion reactions to nanomedicines. Nat Nanotechnol. 2018;13(12):1100–1108. doi:10.1038/s41565-018-0273-130348955
   PubMed Web of Science ®Google Scholar
• Ernsting MJ, Murakami M, Roy A, Li SD. Factors controlling the pharmacokinetics, biodistribution and intratumoral penetration of nanoparticles. J Control Release. 2013;172(3):782–794. doi:10.1016/j.jconrel.2013.09.01324075927
   PubMed Web of Science ®Google Scholar
• Shalini K, Puja K, Pritam KP, Nandini P, Suresh KV, Mallick MA. Gold nanoparticle from andrographis peniculata photosystem II and their in vivo biological effect on embryonic zebrafish (Danio rerio). Environ Nanotechnol Monit Manag. 2019;11:100201. doi:10.1016/j.enmm.2018.100201
   Google Scholar
• Xu C, Zhao X, Wang L, et al. Protein Conjugation with gold nanoparticles: spectroscopic and thermodynamic analysis on the conformational and activity of serum albumin. J Nanosci Nanotechnol. 2018;18(11):7818–7823. doi:10.1166/jnn.2018.15215
   Web of Science ®Google Scholar
• Verma SK, Jha E, Panda PK, et al. Molecular investigation to RNA and protein based interaction induced in vivo biocompatibility of phytofabricated AuNP with embryonic zebrafish. Artif Cells Nanomed Biotechnol. 2018;46(sup3):S671–S684. doi:10.1080/21691401.2018.150574630311784
   PubMed Web of Science ®Google Scholar
• Javed I, Peng G, Xing Y, et al. Inhibition of amyloid beta toxicity in zebrafish with a chaperone-gold nanoparticle dual strategy. Nat Commun. 2019;10(1):3780. doi:10.1038/s41467-019-11762-031439844
   PubMedGoogle Scholar
• Behzadi E, Sarsharzadeh R, Nouri M, et al. Albumin binding and anticancer effect of magnesium oxide nanoparticles. Int J Nanomedicine. 2018;14:257–270. doi:10.2147/IJN.S18642830643405
   PubMed Web of Science ®Google Scholar
• Verma SK, Nisha K, Panda PK, et al. Green synthesized MgO nanoparticles infer biocompatibility by reducing in vivo molecular nanotoxicity in embryonic zebrafish through arginine interaction elicited apoptosis. Sci Total Environ. 2020;713:136521. doi:10.1016/j.scitotenv.2020.13652131951838
   PubMed Web of Science ®Google Scholar
• Dobson CM. Protein folding and misfolding. Nature. 2003;426(6968):884–890. doi:10.1038/nature0226114685248
   PubMed Web of Science ®Google Scholar
• Chetty PS, Mayne L, Lund-Katz S, Englander SW, Phillips MC. Helical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry. Proc Natl Acad Sci U S A. 2017;114(5):968–973. doi:10.1073/pnas.161752311428096372
   PubMed Web of Science ®Google Scholar
• Poirier Y, Grimm A, Schmitt K, Eckert A. Link between the unfolded protein response and dysregulation of mitochondrial bioenergetics in alzheimer’s disease. Cell Mol Life Sci. 2019;76(7):1419–1431. doi:10.1007/s00018-019-03009-430683981
   PubMed Web of Science ®Google Scholar
• von Bergen M, Barghorn S, Biernat J, Mandelkow EM, Mandelkow E. Tau aggregation is driven by a transition from random coil to beta sheet structure. Biochim Biophys Acta. 2005;1739(2–3):158–166. doi:10.1016/j.bbadis.2004.09.01015615635
   PubMed Web of Science ®Google Scholar
• Grassi D, Howard S, Zhou M, et al. Identification of a highly neurotoxic α-synuclein species inducing mitochondrial damage and mitophagy in parkinson’s disease. Proc Natl Acad Sci U S A. 2018;115(11):E2634–E2643. doi:10.1073/pnas.171384911529487216
   PubMed Web of Science ®Google Scholar
• Dettmer U 1, Newman AJ 1, Soldner F 2, et al. Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation. Nat Commun. 2015;6:7314. doi:10.1038/ncomms831426076669
   PubMed Web of Science ®Google Scholar
• Ge X, Yang Y, Sun Y, Cao W, Ding F. Islet amyloid polypeptide promotes amyloid-beta aggregation by binding-induced helix-unfolding of the amyloidogenic core. ACS Chem Neurosci. 2018;9(5):967–975. doi:10.1021/acschemneuro.7b0039629378116
   PubMed Web of Science ®Google Scholar
• Schmidt M, Wiese S, Adak V, et al. Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis. Nat Commun. 2019;10(1):5008. doi:10.1038/s41467-019-13038-z31676763
   PubMedGoogle Scholar
• Liu HL, Wu YC, Zhao JH, et al. Insights into the conformational changes of several human lysozyme variants associated with hereditary systemic amyloidosis. Biotechnol Prog. 2007;23(1):246–254. doi:10.1021/bp060264a17269695
   PubMed Web of Science ®Google Scholar
• Rennella E, Morgan GJ, Yan N, Kelly JW, Kay LE. The role of protein thermodynamics and primary structure in fibrillogenesis of variable domains from immunoglobulin light chains. J Am Chem Soc. 2019;141(34):13562–13571. doi:10.1021/jacs.9b0549931364359
   PubMed Web of Science ®Google Scholar
• Sukhanova A, Poly S, Bozrova S, et al. Nanoparticles with a specific size and surface charge promote disruption of the secondary structure and amyloid-like fibrillation of human insulin under physiological conditions. Front Chem. 2019;7:480. doi:10.3389/fchem.2019.0048031417892
   PubMed Web of Science ®Google Scholar
• Qiong D, Yan Y, Junling G, et al. Targeting ability of antibody-functionalized particles is enhanced by albumin but inhibited by serum coronas. ACS Macro Lett. 2015;4:1259–1263. doi:10.1021/acsmacrolett.5b00627
   PubMed Web of Science ®Google Scholar
• Mirshafiee V, Kim R, Park S, Mahmoudi M, Kraft ML. Impact of protein pre-coating on the protein corona composition and nanoparticle cellular uptake. Biomaterials. 2016;75:295–304. doi:10.1016/j.biomaterials.2015.10.01926513421
   PubMed Web of Science ®Google Scholar
• Mahmoudi M, Lynch I, Ejtehadi MR, Monopoli MP, Bombelli FB, Laurent S. Protein-nanoparticle interactions: opportunities and challenges. Chem Rev. 2011;111(9):5610–5637. doi:10.1021/cr100440g21688848
   PubMed Web of Science ®Google Scholar
• Casals E, Pfaller T, Duschl A, Oostingh GJ, Puntes V. Time evolution of the nanoparticle protein corona. ACS Nano. 2010;4:3623–3632. doi:10.1021/nn901372t20553005
   PubMed Web of Science ®Google Scholar
• Deng ZJ, Mortimer G, Schiller T, Musumeci A, Martin D, Minchin RF. Differential plasma protein binding to metal oxide nanoparticles. Nanotechnology. 2009;20:455101. doi:10.1088/0957-4484/20/45/45510119822937
   PubMed Web of Science ®Google Scholar
• Verma SK, Jha E, Panda PK, et al. Mechanistic insight into size-dependent enhanced cytotoxicity of industrial antibacterial titanium oxide nanoparticles on colon cells because of reactive oxygen species quenching and neutral lipid alteration. ACS Omega. 2018;3(1):1244–1262. doi:10.1021/acsomega.7b0152230023799
   PubMed Web of Science ®Google Scholar
• Lundqvist M, Stigler J, Elia G, et al. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc Natl Acad Sci USA. 2009;105:14265–14270. doi:10.1073/pnas.0805135105
   Web of Science ®Google Scholar
• Monopoli MP, Walczyk D, Campbell A, et al. Physical−chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles. J Am Chem Soc. 2011;133(8):2525–2534. doi:10.1021/ja107583h21288025
   PubMed Web of Science ®Google Scholar
• Cedervall T, Lynch I, Lindman S, et al. 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. doi:10.1073/pnas.060858210417267609
   PubMed Web of Science ®Google Scholar
• Linse S, Cabaleiro-Lago C, Xue WF, et al. Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci USA. 2007;104:8691–8696. doi:10.1073/pnas.070125010417485668
   PubMed Web of Science ®Google Scholar
• Li F, Sarah P. Effect of nanoparticles on protein folding and fibrillogenesis. Int J Mol Sci. 2009;10:646–655.19333426
   PubMed Web of Science ®Google Scholar
• Zia F, Kendall M, Watson SP, Mendes PM. Platelet aggregation induced by polystyrene and platinum nanoparticles is dependent on surface area. RSC Adv. 2018;8(66):37789–37794. doi:10.1039/C8RA07315E30713685
   PubMed Web of Science ®Google Scholar
• Ge C, Du J, Zhao L, et al. Binding of blood proteins to carbon nanotubes reduces cytotoxicity. Proc Natl Acad Sci U S A. 2011;108(41):16968–16973. doi:10.1073/pnas.110527010821969544
   PubMed Web of Science ®Google Scholar
• Khan S, Gupta A, Chaudhary A, Nandi CK. Orientational switching of protein conformation as a function of nanoparticle curvature and their geometrical fitting. J Chem Phys. 2014;141(8):084707. doi:10.1063/1.489344125173030
   PubMed Web of Science ®Google Scholar
• Vertegel AA, Siegel RW, Dordick JS. Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme. Langmuir. 2004;20:6800–6807. doi:10.1021/la049720015274588
   PubMed Web of Science ®Google Scholar
• Shang W, Nuffer JH, Dordick JS, Siegel RW. Unfolding of ribonuclease A on silica nanoparticle surfaces. Nano Lett. 2007;7(7):1991–1995.17559285
   PubMed Web of Science ®Google Scholar
• Lacerda SH, Park JJ, Meuse C, et al. Interaction of gold nanoparticles with common human blood proteins. ACS Nano. 2010;4(1):365–379. doi:10.1021/nn901118720020753
   PubMed Web of Science ®Google Scholar
• Kopp M, Kollenda S, Epple M. Nanoparticle-protein interactions: therapeutic approaches and supramolecular chemistry. Acc Chem Res. 2017;50(6):1383–1390. doi:10.1021/acs.accounts.7b0005128480714
   PubMed Web of Science ®Google Scholar
• Boselli L, Polo E, Castagnola V, Dawson KA. Regimes of biomolecular ultrasmall nanoparticle interactions. Angew Chem Int Ed Engl. 2017;56(15):4215–4218. doi:10.1002/anie.20170034328295888
   PubMed Web of Science ®Google Scholar
• Jia G, Wang H, Yan L, et al. Cytotoxicity of carbon nanomaterials: single-wall nanotube, multi-wall nanotube, and fullerene. Environ Sci Technol. 2005;39:1378–1383. doi:10.1021/es048729l15787380
   PubMed Web of Science ®Google Scholar
• Zeinabad HA, Zarrabian A, Saboury AA, Alizadeh AM, Falahati M. Interaction of single and multi wall carbon nanotubes with the biological systems: tau protein and PC12 cells as targets. Sci Rep. 2016;6:26508. doi:10.1038/srep2650827216374
   PubMed Web of Science ®Google Scholar
• Dahia I, Hanane M, Aicha M, et al. Scattering correlation spectroscopy and raman spectroscopy of thiophenol on gold nanoparticles: comparative study between nanospheres and nanourchins. J Phys Chem C. 2017;121:18254–18262. doi:10.1021/acs.jpcc.7b05355
   Web of Science ®Google Scholar
• Hanane M, Saber J, Djeddi I, et al. Protein corona study by scattering correlation spectroscopy: a comparative study between spherical and urchin-shaped gold nanoparticles. Nanoscale. 2019;11(8):3665–3673. doi:10.1039/C8NR09891C30741295
   PubMed Web of Science ®Google Scholar
• Cha SH, Hong J, McGuffie M, Yeom B, VanEpps JS, Kotov NA. Shape-dependent biomimetic inhibition of enzyme by nanoparticles and their antibacterial Activity. ACS Nano. 2015;9(9):9097–9105. doi:10.1021/acsnano.5b0324726325486
   PubMed Web of Science ®Google Scholar
• Stefan T, Docter D, Kuharev J, et al. Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology. Nat Nanotechnol. 2013;8(10):772–781. doi:10.1038/nnano.2013.18124056901
   PubMed Web of Science ®Google Scholar
• Moyano DF, Liu Y, Peer D, Rotello VM. Rotello modulation of immune response using engineered nanoparticle surfaces. Small. 2016;12(1):76–82. doi:10.1002/smll.20150227326618755
   PubMed Web of Science ®Google Scholar
• Maiorano G, Sabella S, Sorce B, et al. Effects of cell culture media on the dynamic formation of protein–nanoparticle complexes and influence on the cellular response. ACS Nano. 2010;4(12):7481–7491. doi:10.1021/nn101557e21082814
   PubMed Web of Science ®Google Scholar
• Lundqvist M, Stigler J, Cedervall T, et al. The evolution of the protein corona around nanoparticles: a test study. ACS Nano. 2011;5(9):7503–7509. doi:10.1021/nn202458g21861491
   PubMed Web of Science ®Google Scholar
• Ke PC, Lin S, Parak WJ, Davis TP, Caruso FA. Decade of the protein corona. ACS Nano. 2017;11(12):11773–11776. doi:10.1021/acsnano.7b0800829206030
   PubMed Web of Science ®Google Scholar
• Vroman L, Adams AL, Fischer GC, Munoz PC. Interaction of high molecular weight kininogen, factor XII, and fibrinogen in plasma at interfaces. Blood. 1980;55(1):156–159. doi:10.1182/blood.V55.1.156.1567350935
   PubMed Web of Science ®Google Scholar
• Vroman L. Effect of Adsorbed proteins on the wettability of hydrophilic and hydrophobic solids. Nature. 1962;196(4853):476–477. doi:10.1038/196476a013998030
   PubMed Web of Science ®Google Scholar
• Baimanov D, Cai R, Chen C. Understanding the chemical nature of nanoparticle-protein interactions. Bioconjug Chem. 2019;30(7):1923–1937. doi:10.1021/acs.bioconjchem.9b0034831259537
   PubMed Web of Science ®Google Scholar
• Kihara S, van der Heijden NJ, Seal CK, et al. Soft and hard interactions between polystyrene nanoplastics and human serum albumin protein corona. Bioconjug Chem. 2019;30(4):1067–1076. doi:10.1021/acs.bioconjchem.9b0001530821961
   PubMed Web of Science ®Google Scholar
• Winzen S, Schoettler S, Baier G, et al. Complementary analysis of the hard and soft protein corona: sample preparation critically effects corona composition. Nanoscale. 2015;7(7):2992–3001. doi:10.1039/C4NR05982D25599336
   PubMed Web of Science ®Google Scholar
• Weber C, Simon J, Mailänder V, et al. Preservation of the soft protein corona in distinct flow allows identification of weakly bound proteins. Acta Biomater. 2018;76:217–224. doi:10.1016/j.actbio.2018.05.05729885856
   PubMed Web of Science ®Google Scholar
• Ali MS, Altaf M, Al-Lohedan HA. Green synthesis of biogenic silver nanoparticles using Solanum tuberosum extract and their interaction with human serum albumin: evidence of “corona” formation through a multi-spectroscopic and molecular docking analysis. J Photochem Photobiol B. 2017;173:108–119. doi:10.1016/j.jphotobiol.2017.05.01528570906
   PubMed Web of Science ®Google Scholar
• de Barros CHN, Cruz GCF, Mayrink W, Tasic L. Bio-based synthesis of silver nanoparticles from orange waste: effects of distinct biomolecule coatings on size, morphology, and antimicrobial activity. Nanotechnol Sci Appl. 2018;11:1–14. doi:10.2147/NSA.S15611529618924
   PubMed Web of Science ®Google Scholar
• Lynch I, Dawson KA. Protein-nanoparticle interactions. Nano Today. 2008;3(1):40–47. doi:10.1016/S1748-0132(08)70014-8
   Web of Science ®Google Scholar
• Auer S, Trovato A, Vendruscolo M, Hummer G. A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation. PLoS Comput Biol. 2009;5(8):e1000458. doi:10.1371/journal.pcbi.100045819680431
   PubMed Web of Science ®Google Scholar
• Colvin VL, Kulinowski KM. Nanoparticles as catalysts for protein fibrillation. Proc Natl Acad Sci U S A. 2007;104(21):8679–8680. doi:10.1073/pnas.070319410417502593
   PubMed Web of Science ®Google Scholar
• Rocha S, Thünemann AF, Pereira Mdo C, Coelho M, Möhwald H, Brezesinski G. Influence of fluorinated and hydrogenated nanoparticles on the structure and fibrillogenesis of amyloid beta-peptide. Biophys Chem. 2008;137(1):35–42. doi:10.1016/j.bpc.2008.06.01018625543
   PubMed Web of Science ®Google Scholar
• Konar M, Mathew A, Dasgupta S. Effect of silica nanoparticles on the amyloid fibrillation of lysozyme. ACS Omega. 2019;4(1):1015–1026. doi:10.1021/acsomega.8b0316931459377
   PubMed Web of Science ®Google Scholar
• Sung Jean P, Dongwoo K. Conformational changes of fibrinogen in dispersed carbon nanotubes. Int J Nanomed. 2012;7:4325–4333.
   PubMed Web of Science ®Google Scholar
• Zhang T, Tang M, Yao Y, Ma Y. Pu Y MWCNT interactions with protein: surface-induced changes in protein adsorption and the impact of protein corona on cellular uptake and cytotoxicity. Int J Nanomed. 2019;14:993–1009.
   PubMed Web of Science ®Google Scholar
• Spaeth P, Adhikari S, Le L, et al. Circular dichroism measurement of single metal nanoparticles using photothermal imaging. Nano Lett. 2019;19(12):8934–8940. doi:10.1021/acs.nanolett.9b0385331790264
   PubMed Web of Science ®Google Scholar
• Fardanesh A, Zibaie S, Shariati B, et al. Amorphous aggregation of tau in the presence of titanium dioxide nanoparticles: biophysical, computational, and cellular studies. Int J Nanomedicine. 2019;14:901–911.30774341
   PubMed Web of Science ®Google Scholar
• Yadav I, Kumar S, Aswal VK, Kohlbrecher J. Structure and interaction in the ph-dependent phase behavior of nanoparticle-protein systems. Langmuir. 2017;33(5):1227–1238. doi:10.1021/acs.langmuir.6b0412728079383
   PubMed Web of Science ®Google Scholar
• Riek R, Pervushin K, Wüthrich K. TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends Biochem Sci. 2000;25(10):462–468. doi:10.1016/S0968-0004(00)01665-011050425
   PubMed Web of Science ®Google Scholar
• Woods KE, Perera YR, Davidson MB, Wilks CA, Yadav DK, Fitzkee NC. Understanding protein structure deformation on the surface of gold nanoparticles of varying size. J Phys Chem C Nanomater Interfaces. 2016;120(49):27944–27953. doi:10.1021/acs.jpcc.6b0808928348716
   PubMed Web of Science ®Google Scholar
• Shang L, Wang Y, Jiang J, Dong S. pH-Dependent protein conformational changes in albumin: gold nanoparticle bioconjugates: a spectroscopic study. Langmuir. 2007;23:2714–2721. doi:10.1021/la062064e17249699
   PubMed Web of Science ®Google Scholar
• Capomaccio R, Jimenez IO, Colpo P, et al. Determination of the structure and morphology of gold nanoparticle-HSA protein complexes. Nanoscale. 2015;7(42):17653–17657. doi:10.1039/C5NR05147A26462441
   PubMed Web of Science ®Google Scholar
• Ramezani F, Rafii-Tabar H. An in-depth view of human serum albumin corona on gold nanoparticles. Mol Biosyst. 2015;11(2):454–462. doi:10.1039/C4MB00591K25409650
   PubMedGoogle Scholar
• Zhang W, Zhang Q, Wang F, et al. Comparison of interactions between human serum albumin and silver nanoparticles of different sizes using spectroscopic methods. Luminescence. 2015;30(4):397–404. doi:10.1002/bio.274825103628
   PubMed Web of Science ®Google Scholar
• Imaninezhad M, Schober J, Griggs D, Ruminski P, Kuljanishvili I, Zustiak SP. Cell attachment and spreading on carbon nanotubes is facilitated by integrin binding. Front Bioeng Biotechnol. 2018;6:12. doi:10.3389/fbioe.2018.0012929527525
   PubMed Web of Science ®Google Scholar
• Cai X, Ramalingam R, Wong HS, et al. Characterization of carbon nanotube protein corona by using quantitative proteomics. Nanomedicine. 2013;9(5):583–593. doi:10.1016/j.nano.2012.09.00423117048
   PubMed Web of Science ®Google Scholar
• Holt BD, Short PA, Rape AD, Wang YL, Islam MF, Dahl KN. Carbon nanotubes reorganize actin structures in cells and ex vivo. ACS Nano. 2010;4(8):4872–4878. doi:10.1021/nn101151x20669976
   PubMed Web of Science ®Google Scholar
• Sarkar B, Verma SK, Akhtar J, et al. Molecular aspect of silver nanoparticles regulated embryonic development in Zebrafish (Danio rerio) by Oct- 4expression. Chemosphere. 2018;206:560–567. doi:10.1016/j.chemosphere.2018.05.01829778081
   PubMed Web of Science ®Google Scholar
• Verma SK, Jha E, Panda PK, et al. Molecular insights to alkaline based bio-fabrication of silver nanoparticles for inverse cytotoxicity and enhanced antibacterial activity. Mater Sci Eng C Mater Biol Appl. 2018;92:807–818. doi:10.1016/j.msec.2018.07.03730184810
   PubMed Web of Science ®Google Scholar
• Chen M, von Mikecz A. Formation of nucleoplasmic protein aggregates impairs nuclear function in response to SiO2 nanoparticles. Exp Cell Res. 2005;305(1):51–62. doi:10.1016/j.yexcr.2004.12.02115777787
   PubMed Web of Science ®Google Scholar
• Márquez A, Berger T, Feinle A, et al. Bovine serum albumin adsorption on TiO2 colloids: the effect of particle agglomeration and surface composition. Langmuir. 2017;33(10):2551–2558. doi:10.1021/acs.langmuir.6b0378528195734
   PubMed Web of Science ®Google Scholar
• Maiolo D, Bergese P, Mahon E, Dawson KA, Monopoli M. Surfactant titration of nanoparticle-protein corona. Anal Chem. 2014;86(24):12055–12063. doi:10.1021/ac502717625350777
   PubMed Web of Science ®Google Scholar
• Schulze C, Schulze C, Kroll A, et al. Not ready to use overcoming pitfalls when dispersing nanoparticles in physiological media. Nanotoxicology. 2008;2(2):51–61. doi:10.1080/17435390802018378
   Web of Science ®Google Scholar
• My Kieu H, Yoo Jin S, Tae Hyun Y. Effects of agglomeration on in vitro dosimetry and cellular association of silver nanoparticles. Environ Sci Nano. 2018;5:446–455.
   Web of Science ®Google Scholar
• Settanni G, Zhou J, Suo T, et al. Protein corona composition of poly(ethylene glycol)- and poly(phosphoester)-coated nanoparticles correlates strongly with the amino acid composition of the protein surface. Nanoscale. 2017;9(6):2138–2144. doi:10.1039/C6NR07022A28124700
   PubMed Web of Science ®Google Scholar
• Wang J, Bai R, Yang R, et al. Size- and surface chemistry-dependent pharmacokinetics and tumor accumulation of engineered gold nanoparticles after intravenous administration. Metallomics. 2015;7(3):516–524. doi:10.1039/C4MT00340C25671498
   PubMed Web of Science ®Google Scholar
• Dai Q, Walkey C, Chan WC. Polyethylene glycol backfilling mitigates the negative impact of the protein corona on nanoparticle cell targeting. Angew Chem Int Ed Engl. 2014;53(20):5093–5096. doi:10.1002/anie.20130946424700480
   PubMed Web of Science ®Google Scholar
• Schöttler S, Becker G, Winzen S, et al. Protein adsorption is required for stealth effect of poly (ethylene glycol)-and poly (phosphoester)-coated nanocarriers. Nat Nanotechnol. 2016;11(4):372–377. doi:10.1038/nnano.2015.33026878141
   PubMed Web of Science ®Google Scholar
• Cai C, Wang M, Wang L, Wang B, Feng W, Chen C. Thermal unfolding process of lysozyme on PEGylated gold nanoparticles reveals length-dependent effects of PEG layer. J Nanosci Nanotechnol. 2018;18(8):5542–5550. doi:10.1166/jnn.2018.1541629458608
   PubMed Web of Science ®Google Scholar
• Chakraborti S, Sarwar S, Chakrabarti P. The effect of the binding of ZnO nanoparticle on the structure and stability of α-lactalbumin: a comparative study. J Phys Chem B. 2013;117(43):13397–13408. doi:10.1021/jp404411b24044753
   PubMed Web of Science ®Google Scholar
• Deng ZJ, Liang M, Toth I, Monteiro M, Minchin RF. Plasma protein binding of positively and negatively charged polymer-coated gold nanoparticles elicits different biological responses. Nanotoxicology. 2013;7:314–322. doi:10.3109/17435390.2012.65534222394123
   PubMed Web of Science ®Google Scholar
• Fertsch-Gapp S, Semmler-Behnke M, Wenk A, Kreyling WG. Binding of polystyrene and carbon black nanoparticles to blood serum proteins. Inhal Toxicol. 2011;23:468–475. doi:10.3109/08958378.2011.58394421689008
   PubMed Web of Science ®Google Scholar
• Mukhopadhyay A, Basu S, Singha S, Patra HK. Inner-view of nanomaterial incited protein conformational changes: insights into designable interaction. Research. 2018;2018:9712832.
   PubMedGoogle Scholar
• Harush-Frenkel O, Debotton N, Benita S, Altschuler Y. Targeting of nanoparticles to the clathrin-mediated endocytic pathway. Biochem Biophys Res Commun. 2007;353(1):26–32. doi:10.1016/j.bbrc.2006.11.13517184736
   PubMed Web of Science ®Google Scholar
• Zhang LW, Monteiro-Riviere NA. Mechanisms of quantum dot nanoparticle cellular uptake. Toxicol Sci. 2009;110(1):138–155. doi:10.1093/toxsci/kfp08719414515
   PubMed Web of Science ®Google Scholar
• Lunov O, Syrovets T, Loos C, et al. Differential uptake of functionalized polystyrene nanoparticles by human macrophages and a monocytic cell line. ACS Nano. 2011;5(3):1657–1669. doi:10.1021/nn200075621344890
   PubMed Web of Science ®Google Scholar
• Kharazian B, Hadipour NL, Ejtehadi MR. Understanding the nanoparticle-protein corona complexes using computational and experimental methods. Int J Biochem Cell Biol. 2016;75:162–174. doi:10.1016/j.biocel.2016.02.00826873405
   PubMed Web of Science ®Google Scholar
• Gessner A, Lieske A, Paulke BR, Muller RH. Functional groups on polystyrene model nanoparticles: influence on protein adsorption. J Biomed Mater Res A. 2003;65:319–326. doi:10.1002/jbm.a.1037112746878
   PubMed Web of Science ®Google Scholar
• Gessner A, Lieske A, Paulke B, Muller R. Influence of surface charge density on protein adsorption on polymeric nanoparticles: analysis by two-dimensional electrophoresis. Eur J Pharm Biopharm. 2002;54:165–170. doi:10.1016/S0939-6411(02)00081-412191688
   PubMed Web of Science ®Google Scholar
• Böhm G, Muhr R, Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 1992;5:191–195. doi:10.1093/protein/5.3.1911409538
   PubMedGoogle Scholar
• Baler K, Martin OA, Carignano MA, Ameer GA, Vila JA, Szleifer I. Electrostatic unfolding and interactions of albumin driven by pH changes: a molecular dynamics study. J Phys Chem B. 2014;118(4):921–930. doi:10.1021/jp409936v24393011
   PubMed Web of Science ®Google Scholar
• Tsao FHC, Barnes JN, Amessoudji A, Li Z, Meyer KC. Aging-related and gender specific albumin misfolding in alzheimer’s disease. J Alzheimers Dis Rep. 2020;4(1):67–77. doi:10.3233/ADR-20016832328565
   PubMedGoogle Scholar
• Strnad P, McElvaney NG, Lomas DA. Alpha1-antitrypsin deficiency. N Engl J Med. 2020;382(15):1443–1455. doi:10.1056/NEJMra191023432268028
   PubMed Web of Science ®Google Scholar
• Elliott PR, Lomas DA, Carrell RW, Abrahams JP. Inhibitory conformation of the reactive loop of α-1antitrypsin. Nat Struct Biol. 1996;3(8):676–681. doi:10.1038/nsb0896-6768756325
   PubMedGoogle Scholar
• Sziegat F, Wirmer-Bartoschek J, Schwalbe H. Characteristics of human lysozyme and its disease-related mutants in their unfolded states. Angew Chem Int Ed Engl. 2011;50(24):5514–5518. doi:10.1002/anie.20100804021574221
   PubMed Web of Science ®Google Scholar
• Li S, Peng Z, Dallman J, et al. Crossing the blood-brain-barrier with transferrin conjugated carbon dots: a zebrafish model study. Colloids Surf B Biointerfaces. 2016;145:251–256. doi:10.1016/j.colsurfb.2016.05.00727187189
   PubMed Web of Science ®Google Scholar
• Shanghao L, Lingyu W, Charles CC, et al. Nontoxic carbon dots potently inhibit human insulin fibrillation. Chem Mater. 2015;27(5):1764–1771. doi:10.1021/cm504572b
   Web of Science ®Google Scholar
• Zhmurov A, Brown AE, Litvinov RI, Dima RI, Weisel JW, Barsegov V. Mechanism of fibrin(ogen) forced unfolding. Structure. 2011;19(11):1615–1624. doi:10.1016/j.str.2011.08.01322078561
   PubMed Web of Science ®Google Scholar
• Gebauer JS, Malissek M, Simon S, et al. Impact of the nanoparticle-protein corona on colloidal stability and protein structure. Langmuir. 2012;28(25):9673–9679. doi:10.1021/la301104a22524519
   PubMed Web of Science ®Google Scholar
• Hu W, Peng C, Lv M, et al. Protein corona-mediated mitigation of cytotoxicity of graphene oxide. ACS Nano. 2011;5(5):3693–3700. doi:10.1021/nn200021j21500856
   PubMed Web of Science ®Google Scholar
• Ju Y, Dai Q, Cui J, et al. Improving targeting of metal-phenolic capsules by the presence of protein coronas. ACS Appl Mater Interfaces. 2016;8(35):22914–22922. doi:10.1021/acsami.6b0761327560314
   PubMed Web of Science ®Google Scholar
• Kelly PM, Åberg C, Polo E, et al. Mapping protein binding sites on the biomolecular corona of nanoparticles. Nat Nanotechnol. 2015;10(5):472–479. doi:10.1038/nnano.2015.4725822932
   PubMed Web of Science ®Google Scholar
• Brambilla D 1, Verpillot R, Le Droumaguet B, et al. PEGylated nanoparticles bind to and alter amyloid-beta peptide conformation: toward engineering of functional nanomedicines for alzheimer’s disease. ACS Nano. 2012;6(7):5897–5908. doi:10.1021/nn300489k22686577
   PubMed Web of Science ®Google Scholar
• Corbo C, Molinaro R, Taraballi F, et al. Unveiling the in vivo protein corona of circulating leukocyte-like carriers. ACS Nano. 2017;11(3):3262–3273. doi:10.1021/acsnano.7b0037628264157
   PubMed Web of Science ®Google Scholar
• Leibe R, Hsiao IL, Fritsch-Decker S, et al. The protein corona suppresses the cytotoxic and pro-inflammatory response in lung epithelial cells and macrophages upon exposure to nanosilica. Arch Toxicol. 2019;93(4):871–885. doi:10.1007/s00204-019-02422-930838431
   PubMed Web of Science ®Google Scholar
• Escamilla-Rivera V, Uribe-Ramírez M, González-Pozos S, Lozano O, Lucas S, De Vizcaya-ruiz A. Protein corona acts as a protective shield against Fe3O4-PEG inflammation and ROS-induced toxicity in human macrophages. Toxicol Lett. 2016;240(1):172–184. doi:10.1016/j.toxlet.2015.10.01826518974
   PubMed Web of Science ®Google Scholar
• Ebrahim-Habibi MB, Ghobeh M, Aghakhani Mahyari F, Rafii-Tabar H, Sasanpour P. Protein G selects two binding sites for carbon nanotube with dissimilar behavior; a molecular dynamics study. J Mol Graph Model. 2019;87:257–267. doi:10.1016/j.jmgm.2018.12.00730594774
   PubMed Web of Science ®Google Scholar
• Chen X, Wang Y, Wang P. Peptide-induced affinity binding of carbonic anhydrase to carbon nanotubes. Langmuir. 2015;31(1):397–403. doi:10.1021/la504321q25521207
   PubMed Web of Science ®Google Scholar
• Vaitheeswaran S, Garcia AE. Protein stability at a carbon nanotube interface. J Chem Phys. 2011;134(12):125101. doi:10.1063/1.355877621456701
   PubMed Web of Science ®Google Scholar
• Mahendra WIP, Gandhi S, Ju Nie T, et al. Protein/carbon nanotubes interaction: the effect of carboxylic groups on conformational and conductance changes. Appl Phys Lett. 2009;95(7):073704. doi:10.1063/1.3211328
   Web of Science ®Google Scholar
• Liu X, Liu T, Song J, et al. Understanding the interaction of single-walled carbon nanotube (SWCNT) on estrogen receptor: a combined molecular dynamics and experimental study. Ecotoxicol Environ Saf. 2019;172:373–379. doi:10.1016/j.ecoenv.2019.01.10130731268
   PubMed Web of Science ®Google Scholar
• Asuri P, Bale SS, Pangule RC, Shah DA, Kane RS, Dordick JS. Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes. Langmuir. 2007;23(24):12318–12321. doi:10.1021/la702091c17944500
   PubMed Web of Science ®Google Scholar
• Lu N, Sui Y, Tian R, Peng YY. Adsorption of plasma proteins on single-walled carbon nanotubes reduced cytotoxicity and modulated neutrophil activation. Chem Res Toxicol. 2018;31(10):1061–1068. doi:10.1021/acs.chemrestox.8b0014130207453
   PubMed Web of Science ®Google Scholar
• Noordadi M, Mehrnejad F, Sajedi RH, Jafari M, Ranjbar B, Lebedev N. The potential impact of carboxylic-functionalized multi-walled carbon nanotubes on trypsin: a comprehensive spectroscopic and molecular dynamics simulation study. PLoS One. 2018;13(6):e0198519. doi:10.1371/journal.pone.019851929856868
   PubMed Web of Science ®Google Scholar
• Sekar G, Sivakumar A, Mukherjee A, Chandrasekaran N. Existence of hydroxylated MWCNTs demotes the catalysis effect of amylases against starch degradation. Int J Biol Macromol. 2016;86:250–261. doi:10.1016/j.ijbiomac.2016.01.07126812109
   PubMed Web of Science ®Google Scholar
• Yang M, Meng J, Mao X, et al. Carbon nanotubes induce secondary structure changes of bovine albumin in aqueous phase. J Nanosci Nanotechnol. 2010;10(11):7550–7553. doi:10.1166/jnn.2010.282521137980
   PubMed Web of Science ®Google Scholar
• De Paoli SH, Diduch LL, Tegegn TZ, et al. The effect of protein corona composition on the interaction of carbon nanotubes with human blood platelets. Biomaterials. 2014;35(24):6182–6194. doi:10.1016/j.biomaterials.2014.04.06724831972
   PubMed Web of Science ®Google Scholar
• Worrall JW, Verma A, Yan H, Rotello VM. “Cleaning” of nanoparticle inhibitors via proteolysis of adsorbed proteins. Chem Commun (Camb). 2006;22:2338–2340. doi:10.1039/B517421J
   Google Scholar
• Srivastava S, Verma A, Frankamp BL, Rotello VM. Controlled assembly of protein-nanoparticle composites through protein surface recognition. Adv Mater. 2005;17(5):617–621. doi:10.1002/adma.200400776
   Web of Science ®Google Scholar
• Zarabi MF, Farhangi A, Mazdeh SK, et al. Synthesis of gold nanoparticles coated with aspartic acid and their conjugation with FVIII protein and FVIII antibody. Indian J Clin Biochem. 2014;29(2):154–160. doi:10.1007/s12291-013-0323-224757296
   PubMedGoogle Scholar
• Wangoo N, Suri CR, Shekhawat G. Interaction of gold nanoparticles with protein: a spectroscopic study to monitor protein conformational changes. Appl Phys Lett. 2008;92:133104.
   Web of Science ®Google Scholar
• Wangoo N, Bhasin KK, Mehta SK, Suri CR. Synthesis and capping of water-dispersed gold nanoparticles by an amino acid: bioconjugation and binding studies. J Colloid Interface Sci. 2008;323(2):247–254. doi:10.1016/j.jcis.2008.04.04318486946
   PubMed Web of Science ®Google Scholar
• Tsai DH, DelRio FW, Keene AM, et al. Adsorption and conformation of serum albumin protein on gold nanoparticles investigated using dimensional measurements and in situ spectroscopic methods. Langmuir. 2011;27(6):2464–2477. doi:10.1021/la104124d21341776
   PubMed Web of Science ®Google Scholar
• Chaudhary A, Gupta A, Khan S, Nandi CK. Morphological effect of gold nanoparticles on the adsorption of bovine serum albumin. Phys Chem Chem Phys. 2014;16(38):20471–20482. doi:10.1039/C4CP01515K25140357
   PubMed Web of Science ®Google Scholar
• Chakraborty S, Joshi P, Shanker V, Ansari ZA, Singh SP, Chakrabarti P. Contrasting effect of gold nanoparticles and nanorods with different surface modifications on the structure and activity of bovine serum albumin. Langmuir. 2011;27(12):7722–7731. doi:10.1021/la200787t21591651
   PubMed Web of Science ®Google Scholar
• Gagner JE, Lopez MD, Dordick JS, Siegel RW. Effect of gold nanoparticle morphology on adsorbed protein structure and function. Biomaterials. 2011;32(29):7241–7252. doi:10.1016/j.biomaterials.2011.05.09121705074
   PubMed Web of Science ®Google Scholar
• Banerjee V, Das KP. Structure and functional properties of a multimeric protein α-a-crystallin adsorbed on silver nanoparticle surface. Langmuir. 2014;30(16):4775–4783. doi:10.1021/la500700724694218
   PubMed Web of Science ®Google Scholar
• Wang G, Lu Y, Hou H, Liu Y. Probing the binding behavior and kinetics of silver nanoparticles with bovine serum albumin. RSC Adv. 2017;7(15):9393–9401. doi:10.1039/C6RA26089F
   Web of Science ®Google Scholar