1. Abou-Zeid, O.K., Al-Shihi, O.I.K., (2008). Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes. Journal of the American Chemical Society 130, 10793-10801.
2. Abramson, F.P., Lutz, M.P., (1986). The kinetics of induction by rifampin of alpha 1- acid glycoprotein and antipyrine clearance in the dog. Drug Metab Dispos 14, 46-51. 3. Abramson, FP. (1988). Dose-response behavior of the induction of alpha 1-acid
glycoprotein by phenobarbital in the dog. Drug Metab Dispos 16, 546-550.
4. Abriata, L.A., (2011). A simple spreadsheet program to simulate and analyze the far-UV Circular Dichroism spectra of Proteins. J Chem Ed 88, 1268-1273.
5. Aggarwal, P., Hall, J.B., McLeland, C.B., Dobrovolskaia, M.A., McNeil, S.E., (2009). Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv Drug Deliv Rev 61, 428‒437.
6. Aguilar, Z., (2012). Nanomaterials for medical applications. Elsevier Inc. Oxford, UK. 7. Agnihotria, S., Mukherjiabc, S., Mukherji, S., (2014). Size-controlled silver
nanoparticles synthesized over the range 5–100 nm using the same protocol and their antibacterial efficacy. RSC Adv 4, 3974-3983.
8. Ahamed, M., Karns, M., Goodson, M., Rowe, J., Hussain, S.M., Schlager, J.J., Hong, Y., (2008). DNA damage response to different surface chemistry of silver nanoparticles in mammalian cells. Toxicol Appl Pharmacol 233, 404–410.
9. Allen, J.J., Barron, A.R., Bott, S., Bovet, C., Boyd, J., Bratt, A., Chiang, P.T., Cisneros, B., Conn, C., (2012). Introduction to Atomic Absorption Spectroscopy. U: Physical
Methods in Chemistry and Nano Science. Rice University, Houston, Texas.
10. Alexander, J.W. (2009). History of the medical use of silver. Surg. Infect. 10, 289-92. 11. Allen, P.C., Hill, E.A., Stokes, A.M., (1977). Alpha1-acid glycoprotein in plasma
proteins: analytical and preparative techniques. Blackwell Scientific; Oxford, UK.
12. Alvarez-Puebla, R. A., Arceo, E., Goulet, P. J. G., Garrido J. J., Aroca, R. F., (2005). Role of Nanoparticle Surface Charge in Surface-Enhanced Raman Scattering. The
Journal of Physical Chemistry B 109, 3787–3792.
13. Arora, S., Jain, J. M. Rajwade, Paknikar, K.M., (2009). Interactions of silver nanoparticles with primary mouse fibroblasts and liver cells. Toxicol Appl Pharmacol. 236, 310–318.
14. Asharani, P.V., Hande, M.P. (2009). Valiyaveettil, S. Anti-proliferative activity of silver nanoparticles. BMC Cell Biology 17, 10-65.
15. Asharani, P.V., Kah, L., Mun, G., Hande, M.P., Valiyaveettil, S., (2009). Cytotoxicity and genotoxicity of silver nanoparticles in human cells. ACS Nano 3, 279–290.
16. Atkins, P., Julio de Paula., (2009). Physical Chemistry. Eighth Edition. Published in Great Britain by Oxford University Press.
17. Aubert, J.P., Loucheux-Lefebvre, M.H., (1976). Conformational study of alpha1-acid glycoprotein. Arch Biochem Biophys 175, 400-409
18. Auffan, M., Rose J, Wiesner MR, Bottero J-Y., (2009). Chemical stability of metallic nanoparticles: A parameter controlling their potential cellular toxicity in vitro.
Environmental Pollution 157, 1127–1133.
19. Bannunah, A.M., Vllasaliu, D., Lord, L., Stolnik, S., (2014). Mechanisms of Nanoparticle Internalization and Transport Across an Intestinal Epithelial Cell Model: Effect of Size and Surface Charge. Mol. Pharmaceutics 11, 4363–4373.
20. Barbero, F., Russo. L., Vitali, M., Paella, J., Salvo, I., Borrajo, M.L., Busquets-Fité M., Grandori R., Bastús N.G., Casals E., Puntes V., (2017). Formation of the Protein Corona: The Interface between Nanoparticles and the Immune System. Seminars in Immunology 34, 52-60.
21. Baroli, B., Ennas M.G., Loffredo F., Isola M., Pinna R., López-Quintela M.A., (2007). Penetration of metallic nanoparticles in human full-thickness skin. Journal of
Investigative Dermatology 127, 1701-1712.
22. Beaty, R.D., Kerber, J.D., (2002). Concepts, Instrumentation and Techniques in Atomic Absorption Spectrophotometry. The Perkin-Elmer Corporation Norwalk, CT, U.S.A. 23. Beer, C., Foldbjerg, R. Hayashi, Y., Sutherland, D.S., Autrup, H., (2012). Toxicity of
silver nanoparticles - nanoparticle or silver ion? Toxicol Lett 208, 286–292.
24. Benn, T. M. and Westerhoff, P. (2008). Nanoparticle silver released into water from commercially available sock fabrics. Environmental Science & Technology 42, 4133– 4139.
25. Bennemann, K.H., Koutecky, J., (1984). Small Particles and Inorganic Clusters, North Holland, Amsterdam. Small Particles and Inorganic Clusters, Freie Universität Berlin, Germany.
26. Bhol, K.C., Schechter, P.J., (2005). Topical nanocrystalline silver cream suppresses inflammatory cytokines and induces apoptosis of inflammatory cells in a murine model of allergic contact dermatitis. Br. J. Dermatol 152, 1235-1242
27. Bhol, K.C., Schechter, P.J., (2007). Effects of nanocrystalline silver (NPI 32101) in a rat model of ulcerative colitis. Digestive Dis. Sci. 52, 2732-2742.
28. Bilberg, K.,. Hovgaard, M.B., Besenbacher, F., Baatrup, E., (2012). In vivo toxicity of silver nanoparticles and silver ions in zebrafish (Danio rerio). J Toxicol 2012, 293784– 293793.
29. Biou, D., Chanton, P., Konan D., Seta, N., N'Guyen, H., Feger, J., Durand, G., (1989). Microheterogeneity of the carbohydrate moiety of human alpha 1-acid glycoprotein in two benign liver diseases: alcoholic cirrhosis and acute hepatitis. Clin Chim Acta 186, 59-66.
30. Biou, D., Bauvy, C., N'Guyen, H., Codogno, P., Durand, G., Aubery, M., (1991). Alterations of the glycan moiety of human alpha 1-acid glycoprotein in late-term pregnancy. Clin Chim Acta 204, 1-12.
31. Bondarenko, O., Juganson, K., Ivask, A., Kasemets, K., Mortimer, M., Kahru, A. (2013). Toxicity of Ag, CuO i ZnO nanoparticles to selected environmentally relevant test organisms i mammalian cells in vitro: a critical review, Arch. Toxicol. 87, 1181–1200. 32. Borm, P. J., Robbins, D., Haubold, S., Kuhlbusch, T., Fissan, H., Donaldson, K., Schins,
R., Stone, V., Kreyling, W., Lademann, J., Krutmann, J., Warheit, D., Oberdorster, E., (2006). The potential risks of nanomaterials: a review carried out for ECETOC, Particle and Fibre Toxicology 14, 3-11.
33. Boulos, S.P., Davis, T.A., Yang, J.A., Lohse, S. E., Alkilany, A.M., Holland, L. A., Murphy, C.J. (2013). Nanoparticle − Protein Interactions: A Thermodynamic and Kinetic Study of the Adsorption of Bovine Serum Albumin to Gold Nanoparticle Surfaces. Langmuir 29, 14984-14996.
34. Boxall, A.B.A., Chaudhry, Q., Sinclair, C., Jones, A., Aitken, R., Jefferson, B., Watts, C. (2007). Current and future predicted environmental exposure to engineered nanoparticles. Central Science Laboratory, Sand Hutton, York, UK.
35. Branca, M., Gamba, A., Manitto, P., Monti, D., Speranza, G., (1983). The binding of bilirubin to albumin a study using spin-labelled bilirubin. Biochim BiophysActa 742, 341-351.
36. Breaven, G.H., D'Albis, A., and Gratzer, W.B. (1973). EurJBiochem. 33,500-509.
37. Brkić A. L., Milić, M., Pongrac, I.M., Marjanovič, A.M., Mlinarić, H., Pavičić, I., Gajović, S., Vinković Vrček, I., (2017). Impact of surface functionalization on the uptake mechanism and toxicity effects of silver nanoparticles in HepG2 cells. Food and Chemical Toxicology 107, 349-361.
38. Brown, J. R. and Shockley, P., (1982). In Lipid Protein Interactions. (eds Jost, P. and Griffith,O.H.) JohnWiley & Sons, NewYork.
39. Brust, M., Bethell, D., Schiffrin, D.J., Kiely, C.J., (1995). Novel gold dithiol nano‐ networks with non‐metallic electronic properties. Advanced materials 7, 795-797.
40. Brust, M., Walker, M., Bethell, D., Schiffrin, D.J., Whyman, R. (1994). Synthesis of thiol-derivatised gold nanoparticles in a two-phase Liquid–Liquid system. J. Chem. Soc., Chem. Commun 0, 801-802.
41. Burrell, R.E., Heggers, J.P., Davis, G.J., Wright, J.B. (1999). Efficacy of silver-coated dressings as bacterial barriers in a rodent burn sepsis model. Wounds 11, 64-71.
42. Byko, M. (2005). From Electric Corsets to Self-Cleaning Pants: The Materials Science and Engineering of Textiles 57, 14-18.
43. Cantor, C.R., Schimmel, P.R. (1980). Biophysical Chemistry: Part II Techniques for the Study of Biological Structure and Function. W.H. Freeman & Company: Oxford.
44. Capjak, I., Avdičević, Z.M., Sikirić, D.M., Jurašin, D.D., Hozić, A., Pajić, D., Dobrović, S., Goessler, W., Vrček, V.I., (2018). Behavior of silver nanoparticles in wastewater: systematic investigation on the combined effects of surfactants and electrolytes in the model systems. Environmental Science: Water Research & Technology 4, 2146-2159. 45. Carlson, C., Hussain, S.M., Schrand, A.M., Braydich-Stolle, L.K., Hess, K.L., Jones,
R.L., Schlager, J.J., (2008). Unique cellular interaction of silver nanoparticles: size- dependent generation of reactive oxygen species. J Phys Chem B 112, 13608–13619. 46. Carter, D.C. and Ho, J.X., (1994). Structure of serum albumin. Adv Protein Chern 45,
153-203.
47. Casals, E., Pfaller, T., Duschl, A., Oostingh, G.J., Puntes, V. (2010). Time evolution of the nanoparticle protein corona. ACS Nano 2010, 4, 3623–3632.
48. Ceciliani, F. and Pocacqua V. (2007). The acute phase protein alpha1-acid glycoprotein: a modelfor altered glycosylation during diseases. Curr Protein Pept Sci 8, 91-108.
49. Cedervall, T., Lynch I.,, Lindman, S., Berggard, T., Thulin, E., Nilsson, H., Dawson, K. A., Linse., S., (2007). Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci U S A. 104, 2050-2055.
50. Cedervall, T., Lynch I., Foy M., Berggad T., Donnelly S., Cagney G., Linse S., Dawson K. (2007). Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew Chem Int Ed 46, 5754–5756.
51. Chanana, M., Rivera-Gil P., Correa-Duarte M.A., LizMarzán L.M., Parak W.J., (2013). Physicochemical Properties of Protein-Coated Gold Nanoparticles in Biological Fluids and Cells before and after Proteolytic Digestion. Angew Chem Int Ed 52, 4179–4183.
52. Chaturvedi, P.N. and Dave, N.K. (2012). Shah Applications of nano-catalyst in new era. Journal of Saudi Chemical Society 16, 307-325.
53. Chaturvedi, S., Dave, P.N., Shah, N.K. (2012). Applications of nano-catalyst in new era. Journal of Saudi Chemical Society 16, 307–325.
54. Chemistry (2017). Dostupno na:
https://www2.chemistry.msu.edu/faculty/reusch/virttxtjml/spectrpy/UV- VIS/spectrum.htm, (pristupljeno: svibanj 2017.).
55. Chen, Y. H. and Yeh, C.S. (2002). Laser ablation method: use of surfactants to form the dispersed Ag nanoparticles. Colloids and Surfaces A: Physicochemical and Engineering Aspects Volume 197, 133–139.
56. Chen, M., Wang, L.-Y., Han, J.-T., Zhang, J.-Y., Li, Z.-Y., Qian, D.-J. (2006). Preparation and Study of Polyacryamide-Stabilized Silver Nanoparticles through a One- Pot Process. The Journal of Physical Chemistry B 110, 11224–11231.
57. Chernousova, S., Epple, M. (2013). Silver as antibacterial agent: ion, nanoparticle, and metal. Angew Chem Int Ed Engl. 52, 1636-53.
58. Chou, K.S. and Lai, Y.S. (2004). Effect of polyvinyl pyrrolidone molecular weights on the formation of nanosized silver colloids. Mater. Chem. Phys 83, 82-88.
59. Churchman, A.H., Wallace, R., Milne, S.J., Brown, A.P., Brydson, R., Beales, P.A., (2013). Serum albumin enhances the membrane activity of ZnO nanoparticles. Chem Commun 49, 4172–4174.
60. Colombo, S., Buclin, T, Decosterd, L.A., Telenti, A., Furrer, H., Lee B.L., Biollaz, J., Eap, C.B., (2006). Orosomucoid (alpha1-acid glycoprotein) plasma concentration and genetic variants: effects on human immunodeficiency virus protease inhibitor clearance and cellular accumulation. Clin Pharmacol Ther 80, 307-318.
61. Conde, J., Dias, J.T., Grazú, V., Moros, M., Baptista, P.V., de la Fuente, J.M., (2014). Revisiting 30 years of biofunctionalization and surface chemistry of inorganic nanoparticles for nanomedicine. Frontiers Chem 2, 2-48.
62. Corbo, C., Molinaro, R., Parodi, A., Furman, N.E.T., Salvatore, F., Tasciotti, E., (2016). The impact of nanoparticle protein corona on cytotoxicity, immunotoxicity and target drug delivery. Nanomedicine 11(1):81–100.
63. Cui, M.H., Liu, R.X., Deng, Z.Y., Ge, G.L., Liu, Y., Xie, L.M., (2014). Quantitative Study of Protein Coronas on Gold Nanoparticles with Different Surface Modifications Nano Research 7, 345–352.
64. Curry S. (2009). Lessons from the crystallographic analysis of the small molecule binding to human serum albumin. Drug Metab Pharmacokinet 24, 342-57.
65. Curry, S., Brick, P., Franks, N.P., (1999). Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochimica et Biophysica Acta 1441, 131- 140
66. Cushing, B.L., Kolesnichenko, V.L. , O’Connor, C.J., (2004). Recent Advances in the Liquid-Phase Syntheses of Inorganic Nanoparticles. Chem.Rev 104, 3893-3946.
67. Diederichs J.E. (1996). Plasma protein adsorption patterns on liposomes: establishment of analytical procedure. Electrophoresis 17, 607–611.
68. Ding, F., Radic, S., Chen, R., Chen, P., Geitner, N.K., Brown, J.M., Ke, P. C., (2013). Direct observation of a single nanoparticle-ubiquitin corona formation. Nanoscale 5, 9162–9169.
69. Docter, D., Westmeier, D., Markiewicz, M., Stolte, S., Knauer, S.K., Stauber, R.H., (2015). The nanoparticle biomolecule corona: lessons learned– challenge accepted? Chem. Soc. Rev 44, 6094-6121.
70. Dominguez-Medina, S., Blankenburg, J., Olson, J., Landes, C.F., Link, S. (2013). Adsorption of a Protein Monolayer via Hydrophobic Interactions Prevents Nanoparticle Aggregation under Harsh Environmental Conditions. ACS Sustainable Chem Eng 7, 833–842.
71. Duche, J.C., Urien, S., Simon, N., Malaurie, E., Monnet, I., Barre, J., (2000). Expression of the genetic variants of human alpha-1-acid glycoprotein in cancer. Clin Biochem 33, 197-202.
72. Duncan, T.V. (2011). “Applications of nanotechnology in food packaging and food safety: barrier materials, antimicrobials and sensors”, J Colloid Interface Sci 363, 1-24. 73. Duran, N., Silveira, C.P., Duran, M., Martinez, D., (2015). Silver nanoparticle protein
corona and toxicity: a mini-review. Journal of Nanobiotechnology 13, 55-72.
74. Durán, N., Durán, M., Seabra, A.B., Fávaro, W.J., Nakazato, G., (2016). Silver nanoparticles: a new view on mechanistic aspects on antimicrobial activity. Nanomed. Nanotechnol. Biol. Med. 12, 789–799.
75. Dziendzikowska, K., Gromadzka-Ostowska, J., Lankoff, A., Oczkowski, M., Krawczyńska, A., Chwastowska, J., Sadowska-Bratek, M., Chajduk, E., Wojewódzka, M., Dušinská, M., Kruszewski, M., (2012). Time-dependent biodistribution and excretion of silver nanoparticles in male. Wistarrats. J. Appl. Toxicol 32, 920–928.
76. Eap, C.B., Fischer, J.F., Baumann, P., (1991). Variations in relative concentrations of variants ofhuman alpha 1-acid glycoprotein after acute-phase conditions. Clin Chim Acta 203, 379-385.
77. Eigler, D.M. and Schweizer E.K. (1990). Positioning single atoms with a scanning tunnelling microscope. Nature 344, 524-526.
78. El-Badawy, A., Feldhake, R., Venkatapathy, R., (2010). State-Of-The-Science Review: Everything NanoSilver and More. U.S. Environmental Protection Agency, Washington. 79. El-Badawy, A.M., Silva, R.G., Morris, B., Scheckel, K.G., Suidan, M.T., Tolaymat,
T.M. (2011). Surface Charge-Dependent Toxicity of Silver Nanoparticles. Environ. Sci. Technol. 45, 283-287.
80. Elechiguerra, J.L., Burt, J.L., Morones, J.R, Camacho-Bragado, A., Gao, X., Lara, H.H., Yacaman, M.J., (2005). Interaction of silver nanoparticles with HIV-1. Journal of Nanobiotechnology 3, 6-16.
81. Elliott, H.G., Elliott, M.A., Watson, J, Steele, L, Smith, K.D., (1995). Chromatographic Investigation of the Glycosylation Pattern of Alpha-1-Acid Glycoprotein Secreted by the HEPG2 Cell Line; a Putative Model for Inflammation. Biomed Chrom 9, 199-204. 82. Elzey, S. and Grassian, V.H., (2010). Agglomeration, isolation and dissolution of
commercially manufactured silver nanoparticles in aqueous environments. Journal of Nanoparticle Research 12, 1945–1958.
83. Empa & TSV Schweiz Textilverband. (2011). Nano textiles – Grundlagen und Leitprinzipien zur effizienten Entwicklung nachhaltiger Nanomaterialien, Ausga
84. Enciklopedija (2017). Dostupno na:
http://www.enciklopedija.hr/natuknica.aspx?ID=4486#top, pristup travanj 2017.
85. Eskandari, K., Kamali, M., Ramezani, M., Safiri, Z., Keihan, A.H., Rashidiani, J., Kooshki, H, Zarei, H., (2013). The Effect of Hydrophobicity and Hydrophilicity of Gold Nanoparticle on Proteins Structure and Function. International Journal of Bio-Inorganic Hybrid Nanomaterials 3, 465-470
86. European Commission (2011). Commission Recommendation on the definition of nanomaterial. Official Journal of the European Union, Brussels.
87. European Commission (2013). Communication from the Commission to the European Parliament, the Council and the European Economic and Social Committee. Second regulatory review on nanomaterials. Brussels.
88. European Commission (2014). Communication from the Scientific Committee on Emerging and Newly Identified Health Risks (SCENIHR). Opinion on Nanosilver:
safety, health and environmental effects and role in antimicrobial resistance. Brussels, effects and rolein antimicrobial resistance. Brussels.
89. European Commission (2015). Communication from the Scientific Committee on Emerging and Newly Identified Health Risks (SCENIHR). Opinion on the Guidance on the Determination of Potential Health Effects of Nanomaterials Used in Medical Devices. Brussels.
90. Evans, F., Wennerstrom, H., (1994). Polymers in Colloidal Systems. In The Colloidal Domain: Where Physics, Chemistry, Biology, and Technology Meet; Wiley-VCH: New York.
91. Fan, L. and Guo, R., (2008). Growth of Dendritic Silver Crystals in CTA/SDBS Mixed- Surfactant Solutions. Crystal Growth & Design 8, 2150–2156.
92. Fey, G.H., Fuller, G.M. (1987). Regulation of acute phase gene expression by inflammatory mediators. Mol Biol Med 4, 323-338.
93. Filip, Z., Jan, K., Vendula, S., Jana, K. Z., Kamil, M., Kamil, K., (2013). Albumin and α1-acid glycoprotein: old acquaintances. Expert Opin Drug Metab Toxicol 9, 943-954. 94. Filipović, I., Lipanović, S. (1987). Opća i anorganska kemija. Školska knjiga, Zagreb. 95. Finsy, R., (1994). Particle sizing by quasi-elastic light-scattering. Adv. Colloid Interface
Sci 52, 79–143.
96. Fleischert, C.C. and Payne, C.K., (2014). Nanoparticle–Cell Interactions: Molecular Structure of the Protein Corona and Cellular Outcomes. Acc. Chem. Res 47, 2651–2659. 97. Fornes, J.A. (1985). Secondary minimum analysis in the DLVO theory. Colloid Polym
Sci 263, 1004–1007.
98. Fournier, T., Medjoubi, N.N., Porquet, D., (2000). Alpha-1-acid glycoprotein. Biochim Biophys Acta 1482, 157-171.
99. Fournier, T., Vranckx, R., Mejdoubi, N., Durand, G., Porquet, D., (1994). Induction of rat alpha-1-acid glycoprotein by phenobarbital is independent of a general acute-phase response. Biochem Pharmacol 48, 1531-1535.
100. Gamer, A.O., Leibold, E., Van-Ravenzwaay, B. (2006). The in vitro absorption of microfine zinc oxide and titanium dioxide through porcine skin. Toxicology in Vitro 3, 301-307.
101. Gebauer, J.S., Malissek, M., Simon, S., Knauer, S.K., Maskos, M., Stauber, R.H., Peukert, W., Treuel, L. (2012). Impact of the Nanoparticle–Protein Corona on Colloidal Stability and Protein Structure. Langmuir 28, 9673–9679.
102. Generalić, E. (2017). "Zeta potencijal." Englesko-hrvatski kemijski rječnik. Dostupno na: https://glossary.periodni.com/dictionary.php?en=zeta+potencijal, (prostupljeno: svibanj 2017.)
103. Georgios, A.S. and Sotiris, E., (2011). Pratsinis Engineering nanosilver as an antibacterial, biosensor and bioimaging material. Curr Opin Chem Eng 1, 3–10.
104. Goesmann, H. and Feldmann, C., (2010). Nanoparticulate Functional Materials. Angew Chem Int Ed 49, 1362–1395.
105. Goppert, T.M. and Muller, RH., (2005). Adsorption kinetics of plasma proteins on solid lipid nanoparticles for drug targeting. Int J Pharm 302, 172–186.
106. Gornik, O. and Lauc, G., (2008). Glycosylation of serum proteins in inflammatory diseases. Dis Markers 25, 267–278.
107. Grand View Research, Report. (2015). Silver Nanoparticles Market By Application (Electronics & electrical, healthcare, food & beverages, textiles) and segment forecasts to 2022.
108. Gray, R.D. and Stroupe, S.D., (1978). Kinetics and mechanism of bilirubin binding to human serum albumin. J Biol Chem 25, 4370–4377.
109. Greenfield, N.J. (2006). Using Circular Dichroism spectra to estimate protein secondary structure. Nat. Protoc 1, 2876-2890.
110. Gurunathan, S., Han, J.W., Kwon, D.N., Kim, J.H., (2014). Enhanced antibacterial and antibiofilm activities of silver nanoparticles against Gram-negative and Gram-positive bacteria. Nanoscale Res. Lett. 9, 373-390.
111. Guzmán, M.G., Dille, J., Godet, S. (2009). Synthesis of silver nanoparticles by chemical reduction method and their antibacterial activity. International Journal of Chemical and Biomolecular Engineering 2, 3-11.
112. Hackenberg, A., Scherzed, A., Kessler, M., Hummel, S., Technau, A., Froelich, K., Ginzkey, C., Koehler, C., Hagen, R., Kleinsasser, N., (2011). Silver nanoparticles: evaluation of DNA damage, toxicity and functional impairment in human mesenchymal stem cells. Toxicol Lett 201, 27–33.
113. Hage, D.S. and Austin, J., (2000). High-performance affinity chromatography and immobilized serum albumin as probes for drug - and hormone-binding. J Chromatogr B Biomed Sci Appl 739, 39-54.
114. Hanada, K., Yamanaka, E., Yamamoto, N., Minami, H., Kawai, S., Sasaki Y., Ogata, H., (2011). Effects of surgery and chronic disease states on the concentrations and phenotype
distribution of alpha1-acid glycoprotein: studies in patients with breast cancer and patients with chronic inflammatory disease. Int J Clin Pharmacol Ther 49, 415-421. 115. Hashimoto, S., Asao, T., Takahashi, J., Yagihashi, Y., Nishimura, T., Saniabadi, A.R.,
Poland, D.C., van Dijk, W., Kuwano, H., Kochibe, N., Yazawa, S., (2004). alpha1-acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis. Cancer 101, 2825-2836.
116. Hassan, P.A., Rana, S., Verma, G. (2015) Making sense of Brownian motion: colloid characterization by dynamic light scattering. Langmuir 31, 3-12.
117. Hayashi, T., Era, S., Kawai, K, Imai, H., Nakamura, K., Onda, E., Yoh, M., (2000). Observation for redox state of human serum and aqueous humor albumin from patients with senile cataract. Pathophysiology 6, 237-43.
118. He, D., Dorantes-Aranda, J.J., Waite, T.D. (2012). Silver Nanoparticle-Algae Interactions: Oxidative Dissolution, Reactive Oxygen Species Generation and Synergistic Toxic Effects. Environ Sci Technol 46, 8731–8738.
119. Hedberg, J., Lundin, M., Lowe, T., Blomberg, E., Wold, S., Wallinder, I.O., (2012). Interactions between surfactants and silver nanoparticles of varying charge. Journal of Colloid and Interface Science 369, 193–201.
120. Hegyi, G., Kardos, J., Kovács, M., Málnási-Csizmadia, A., Nyitray, L., Pál, G., Radnai, L., Reményi, A., Venekei, I., (2013). Molecular forces stabilising ligand binding. U: Introduction to Practical Biochemistry. ELTE Faculties of Science Student Foundation, Eötvös Loránd University, Macarska.
121. Henglein, A. (1998). Colloidal Silver Nanoparticles: Photochemical Preparation and Interaction with O2, CCl4, and Some Metal Ions. Chem. Mater 10, 444–540.
122. Higai, K., Aoki, Y., Azuma, Y, Matsumoto, K. (2005). Glycosylation of site-specific glycans of α1-acid glycoprotein and alterations in acute and chronic inflammation. Biochim Biophys Acta 1725, 128-135.
123. Hochepied, T., Berger, F.G., Baumann, H., Libert, C., (2003). Alpha(1)-acid glycoprotein: an acute phase protein with inflammatory and immunomodulating properties. Cytokine Growth Factor Rev 14, 25-34.
124. Hotze, E.M., Labille, J., Alvarez, P., Wiesner, M.R., (2008). Environ Sci Technol 42, 4175–4180.
125. Huang, R., Carney, R.P., Stellacci, F., Lau, B.L.T., (2013). Protein–nanoparticle interactions: the effects of surface compositional and structural heterogeneity are scale dependent. Nanoscale 5, 6928-6935.
126. Hunter, R.J. (2001). Double Layer Interaction and Particle Coagulation. InFoundations of Colloid Science, 2nd ed.; Oxford University Press: NewYork.
127. Hussain, S.M., Braydich-Stolle, L.K., Schrand, A.M., Murdock, R.C., Yu, K.O., Mattie, D.M., Schlager, J.J., Terrones, M. (2009). Adv Mater 21, 1549–1559.
128. Israili, Z.H and Dayton, PG., (2001). Human alpha-1-glycoprotein and its interactions with drugs. Drug Metab Rev 33, 161-235.
129. Janes, R.W. (2005). Bioinformatics analyses of Circular Dichroism protein reference databases. Bioinformatics 21, 4230-4238.
130. Jezequel, M., Set,a N.S., Corbic, M.M., Feger, J.M., Durand, G.M. (1988). Modifications of concanavalin A patterns of alpha 1-acid glycoprotein and alpha 2-HS glycoprotein in alcoholic liver disease. Clin Chim Acta 176, 49-57.
131. Jiang, J., Oberdörster, G., Biswas, P. (2009). Characterization of size, surface charge, and agglomeration state of nanoparticle dispersions for toxicological studies. J. Nanopart. Res 11, 77–89.
132. Jhonsi, M.A., Kathiravan, A., Renganathan, R. (2009). Spectroscopic studies on the interaction of colloidal capped CdS nanoparticles with bovine serum albumin. Colloids Surf B Biointerfaces 72, 167–172.
133. Joseph, K.S., Moser, A.C., Basiaga, S.B.G., Schiel, J.E., Hage, D.S., (2009). Evaluation of alternatives to warfarin as probes for Sudlow site I of human serum albumin: characterization by high-performance affinity chromatography. J Chromatogr A 1216, 3492-500.
134. Jurašin, D., Dutour Sikirić, M. (2014). Higher Oligomeric Surfactants — From Fundamentals to Applications, in Oligomerization of Chemical i Biological Compounds, InTech.
135. Jurašin, D.D., Čurlin, M., Capjak, I., Crnković, T., Lovrić, M., Babič, M., Horàk, D., Vrček I.V., (2016). Sufrace coating affects behavior of metalic nanoparticle in a bilogical environment. Beilstein Journal of Nanotechnology 7, 246-262.
136. Kaiser, J.P., Roesslein, M., Diener, L., Wichser, A., Nowack, B., Wick. P. (2017). Cytotoxic effects of nanosilver are highly dependent on the chloride concentration and the presence of organic compounds in the cell culture media. J Nanobiotechnology 15, 5- 16.
137. Kato, H. (2012). Size Determination of Nanoparticles by Dynamic Light Scattering, Nanomaterials: Processing and Characterization with Lasers, Subhash Chandra Singh, Haibo Zeng, Chunlei Guo, and Weiping Cai, Wiley-VCH Verlag GmbH & Co.
138. Kelly, S.M., Jess, T.J., Price, N.C., (2005). How to study proteins by Circular Dichroism. Biochimica et Biophysica Acta 1751, 119-139.
139. Khan, Z., Al-Thabaiti, S.A, Obaid, Y.A., Al-Youbi, A.O., (2011). Preparation and characterization of silver nanoparticles by chemical reduction method. Colloids and Surfaces B: Biointerfaces 82, 513–517.
140. Khrapunov, S. (2009). Circular dichroism spectroscopy has intrinsic limitations for protein secondary structure analysis. Anal Biochem 389, 174-176
141. Kim, H.R., Andrieux, K., Delomenie, C., Chacun, H., Appel, M., Desmaele, D., Taran, F., Georgin, D., Couvreur, P., Taverna, M,. (2007). Analysis of plasma protein adsorption onto PEGylated nanoparticles by complementary methods: 2-DE, CE and Protein Labon-chip system. Electrophoresis 28, 2252–2261.
142. Kim, H.S. and Wainer, I.W., (2008). Rapid analysis of the interactions between drugs and human serum albumin (HSA) using high-performance affinity chromatography (HPAC). J Chromatogr B Biomed Sci Appl 870, 22-26.
143. Kim, J.S., Kuk, E., Yu, K.N., Kim, J.H., Park, S.J., Lee, H.J., Kim, S.H., Park, Y.H., Hwang, C.Y., Kim, Y.K., Lee, Y.S., Jeong, D.H., Cho, M.H., (2007). Antimicrobial effects of silver nanoparticles. Nanomed. Nanotechnol. Biol. Med 3, 95–101.
144. Kirsch, R., Frith, L., Black, E., Hoffenberg, R., (1968). Regulation of albumin synthesis and catabolism by alteration of dietary protein. Nature 217,578-579.
145. Kittler, S., Greulich, C., Gebauer, J.S., Diendorf, J., Treuel, L., Ruiz, L., Gonzalez- Calbet, J. M., Vallet-Regi, M, Zellner, R., Koller, M., Epple, M., (2010). The influence of proteins on the dispersability and cell-biological activity of silver NP. Journal of Materials Chemistry 20, 512-518.
146. Klein, J. (2007). Probing the interaction of proteins and nanoparticles. PNAS 104, 2029- 2030.
147. Klevens, R.M., Edwards, J.R., Richards, C.L.Jr, Horan, T.C., Gaynes, R.P., Pollock, D.A., Cardo, D.M., (2007). Estimating health care-associated infections and deaths in US hospitals. Public Health Rep 122, 160-166.
148. Kopecky, V.Jr., Ettrich, R., Hofbauerova, K., Baumruk, V., (2003). Structure of human alpha1-acid glycoprotein and its high-affinity binding site. Biochem Biophys Res Commun 300, 41-46.
149. Korbekandi, S.I. (2012). Nanotechnology and Nanomaterials » "The Delivery of Nanoparticles", Chapter 1 Silver Nanoparticles. InTech, Rijeka, Croatia.
150. Koshkina, O., Lang, T., Thiermann, R., Docter, D., Roland, H.S., Secker, C., Schlaad, H., Weidner, S., Mohr, B., Maskos, M., Bertin, A., (2015). Temperature-Triggered Protein Adsorption on Polymer-Coated Nanoparticles in Serum. Langmuir 31, 8873−8881.
151. Kragh-Hansen, U. (1983). Relations between high-affinity binding sites for L- tryptophan, diazepam, salicylate and Phenol Red on human serum albumin. Biochem J 209, 135-4.
152. Kragh-Hansen, U., Chuang, V.T.G, Otagiri, M., (2002). Practical aspects of the ligand- binding and enzymatic properties of human serum albumin. Biol Pharm Bull 25, 695- 704.
153. Kratochwil, N.A., Huber, W., Mueller, F., Kansy, M., Gerber, P.R., (2004). Predicting plasma protein binding of drugs – revisited. Curr Opin Drug Discov Devel 4, 507-512. 154. Kremer, J.M., Wilting, J., Jansen, L.H., (1988). Drug binding to human alpha 1-acid
glycoprotein in health and disease Pharmacol Rev 40, 1-47.