Bioactivity of albumins bound to silver nanoparticles

Protein Journal

Volumn 33, Issue 3, 2014, Pages 258-266

  Mariam, Jessy ^a   Sivakami, S ^a   Kothari, D C ^a   Dongre, P M ^a  

^a UNIVERSITY OF MUMBAI   (India)

Author keywords

Albumins; Antioxidant property; Copper binding; Drug binding; Esterase activity; Silver nanoparticles

Indexed keywords

BOVINE SERUM ALBUMIN; ESTERASE; HUMAN SERUM ALBUMIN; IBUPROFEN; SILVER NANOPARTICLE; THIOL GROUP; WARFARIN; 2,2'-AZOBIS(2-AMIDINOPROPANE); ALBUMINOID; AMIDINE; COPPER; METAL NANOPARTICLE; NANOPARTICLE; PROTEIN BINDING; SILVER;

ANTIOXIDANT ACTIVITY; ARTICLE; BIOLOGICAL ACTIVITY; CATALYSIS; CIRCULAR DICHROISM; DRUG BINDING; ENZYME ACTIVITY; ENZYME KINETICS; HEMOLYSIS; PROTEIN BINDING; ANIMAL; BOVINAE; CHEMISTRY; HUMAN; METABOLISM;

BOVINAE;

ALBUMINS; AMIDINES; ANIMALS; CATTLE; COPPER; ESTERASES; HUMANS; METAL NANOPARTICLES; NANOPARTICLES; PROTEIN BINDING; SERUM ALBUMIN, BOVINE; SILVER;

EID: 84902880281     PISSN: 15723887     EISSN: 18758355     Source Type: Journal    
DOI: 10.1007/s10930-014-9553-2     Document Type: Article

References (60)

1. Treuel L, Brandholt S, Maffre P, Wiegele S, Shang L, Nienhaus G (2014) Impact of protein modification on the protein corona on nanoparticles and nanoparticle-cell interactions. ACS Nano 8(1):503-513
2. Cedervall T, Lynch I, Lindman S, Berggård T, Thulin E, Nilsson H, Dawson KA, Linse S (2007) Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA 104(7):2050-2055 (Pubitemid 46391350)
3. Milani S, Bombelli F, Pitek A, Dawson K, Rädler J (2012) Reversible versus irreversible binding of transferrin to polystyrene nanoparticles: soft and hard corona. ACS Nano 6(3):2532-2541
4. 2) nanoparticles. Small 7(24):3479-3486
5. Monopoli MP, Aberg C, Salvati A, Dawson KA (2012) Biomolecular coronas provide the biological identity of nanosized materials. Nat Nano 7(12):779-786
6. Monopoli M, Bombelli F, Dawson K (2012) Nanobiotechnology: nanoparticle coronas take shape. Nat Nano 6(1):11-12
7. Salvati A, Aberg C, dos Santos T, Varela J, Pinto P, Lynch I, Dawson KA (2011) Experimental and theoretical comparison of intracellular import of polymeric nanoparticles and small molecules: toward models of uptake kinetics. Nanomedicine 7(6):818-826
8. Tenzer S, Docter D, Kuharev J, Musyanovych A, Fetz V, Hecht R, Schlenk F, Fischer D, Klytaimnistra Kiouptsi K, Reinhardt C, Landfester K, Schild H, Maskos M, Knauer SK, Stauber RH (2013) Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology. Nat Nano 8:772-781
9. Monteiro-Riviere N, Samberg M, Oldenburg S, Riviere J (2013) Protein binding modulates the cellular uptake of silver nanoparticles into human cells: implications for in vitro to in vivo extrapolations? Toxicol Lett 220(3):286-293
10. Monopoli M, Walczyk D, Campbell A, Elia G, Lynch I, Bombelli F, Dawson K (2011) Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles. J Am Chem Soc 133:2525-2534
11. Gebauer J, Malissek MM, Simon SS, Knauer S, Maskos M, Stauber R, Peukert W, Treuel L (2012) Impact of the nanoparticle-protein corona on colloidal stability and protein structure. Langmuir 28:9673-9679
12. Cabaleiro-Lago C, Quinlan-Pluck F, Lynch I, Dawson K, Linse S (2010) Dual effect of amino modified polystyrene nanoparticles on amyloid b protein fibrillation. ACS Chem Neurosci 1(4):279-287
13. Wigginton N, Titta A, Piccapietra F, Dobias J, Nesatyy V, Suter M, Bernier-Latmani R (2010) Binding of silver nanoparticles to bacterial proteins depends on surface modifications and inhibits enzymatic activity. Environ Sci Technol 44:2163-2168
14. Wen Y, Geitner N, Chen R, Ding F, Chen P, Andorfer R, Govindan PN, Ke PC (2013) Binding of cytoskeletal proteins with silver nanoparticles. RSC Adv 3:22002-22007
15. Banerjee V, Das K (2013) Interaction of silver nanoparticles with proteins: a characteristic protein concentration dependent profile of SPR signal. Colloids Surf B 111:71-79
16. Mariam J, Dongre PM, Kothari DC (2011) Study of interaction of silver nanoparticles with bovine serum albumin using fluorescence spectroscopy. J Fluoresc 21:2193-2199
17. Xingcan S, Qi Y, Hong L, Haigang Y, Xiwen H (2003) Hysteresis effects of the interaction between serum albumins and silver nanoparticles. Sci China Ser B 64:387-398
18. Ravindran A, Singh A, Raichur A, Chandrasekaran N, Mukherjee A (2010) Studies on interaction of colloidal Ag nanoparticles with bovine serum albumin (BSA). Colloids Surf B 76:32-37
19. Peters T (1996) All about albumin: biochemistry, genetics and medical applications. Academic Press, San Diego
20. Means G, Bender M (1975) Acetylation of human serum albumin by p-nitrophenyl acetate. Biochemistry 14:4989-4994
21. Agarwal R, Phillips M, McPherson R, Hensley P (1986) Serum albumin and the metabolism of disulfiram. Biochem Pharmacol 35:3341-3347 (Pubitemid 16001444)
22. Roche M, Rondeau P, Singh N, Tarnus E, Bourdon E (2008) The antioxidant properties of serum albumin. FEBS Lett 582:1783-1787
23. Pramanik S, Banerjee P, Sarkar A, Bhattacharya S (2008) Size-dependent interaction of gold nanoparticles with transport protein: a spectroscopic study. J Lumin 128:1969-1974
24. Bhogale A, Patel N, Sarpotdar P, Mariam J, Dongre PM, Miotello A, Kothari DC (2013) Systematic investigation on the interaction of bovine serum albumin with ZnO nanoparticles using fluorescence spectroscopy. Colloids Surf B 102:257-264
25. Yang Q, Liang J, Han H (2009) Probing the interaction of magnetic iron oxide nanoparticles with bovine serum albumin by spectroscopic techniques. J Phys Chem B 113:10454-10458
26. Gaoa D, Tian YY, Liang F, Ding L, Bi S, Chen Y, Zhang HH, Yu A (2006) Investigation on the interaction between colloidal gold and human complement factor 4 at different pH by spectral methods. Colloids Surf B 47:71-77 (Pubitemid 43111607)
27. Lara H, Garza-Treviño E, Ixtepan-Turren L, Singh D (2011) Silver nanoparticles are broad-spectrum bactericidal and virucidal compounds. J Nanobiotechnol 9:30
28. Shrivastava S, Bera T, Singh KS, Singh G, Ramchandrarao P, Dash D (2009) Characterization of antiplatelet properties of silver nanoparticles. ACS Nano 3:1357-1364
29. Lee P, Meisel D (1982) Adsorption and surface enhanced Raman of dyes on silver and gold sols. J Phys Chem 86:3391-3395
30. Ellman G (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-77
31. Riddles P, Blakeley R, Zerner B (1979) Ellman's reagent: 5, 5′-dithiobis(2-nitrobenzoic acid) - a reexamination. Anal Biochem 94:75-81 (Pubitemid 9170207)
32. Sato Y, Kamo S, Takahashi T, Suzuki Y (1995) Mechanism of free radical-induced hemolysis of human erythrocytes: hemolysis by water-soluble radical initiator. Biochemistry 34:8940-8949
33. Smith G, Wilkins D (1953) New colorimetric reagent specific for copper: determination of copper and iron. Anal Chem 25:510-511
34. Shaw A, Pal S (2008) Spectroscopic studies on the effect of temperature on pH-induced folded states of human serum albumin. J Photochem Photobiol B 90:69-77
35. Treuel L, Malissek M, Gebauer J, Zellner R (2010) The influence of surface composition of nanoparticles on their interactions with serum albumin. Chem Phys Chem 11:3093-3099
36. Kiselev M, Gryzunov I, Dobretsov G, Komarova M (2001) Size of a human serum albumin molecule in solution. Biofizika 46:423-427
37. Hawe A, Hulse W, Jiskoot W, Forbes R (2011) Taylor dispersion analysis compared to dynamic light scattering for the size analysis of therapeutic peptides and proteins and their aggregates. Pharm Res 28:2302-2310
38. Lockridge O, Xue W, Gaydess A, Grigoryan H, Ding S, Schopfer L, Hinrichs S, Masson P (2008) Pseudo-esterase activity of human albumin. J Biol Chem 283:22582-22590
39. Georges H, Presle N, Buronfosse T, Fournel-Gigleux S, Netter P, Magdalou J, Lapicque F (2000) In vitro stereoselective degradation of carprofen glucuronide by human serum albumin. Characterization of sites and reactive amino acids. Chirality 12:53-62 (Pubitemid 30068905)
40. Aliaga A, Osorio-Roman I, Garrido C, Leyton P, Cárcamo J, Clavijo E, Gómez-Jeria J, Díaz G, Campos-Vallette M (2009) Surface enhanced Raman scattering study of L-lysine. Vib Spectrosc 50:131-135
41. Watanabe H, Tanase S, Nakajou K, Maruyama T, Kragh-Hansen U, Otagiri M (2000) Role of Arg-410 and Tyr-411 in human serum albumin for ligand binding and esterase-like activity. Biochem J 349:813-819 (Pubitemid 30609413)
42. Sakurai Y, Ma S, Watanabe H, Yamaotsu N, Hirono S, Kurono Y, Kragh-Hansen U, Otagiri M (2004) Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates. Pharm Res 21:285-292 (Pubitemid 38221974)
43. Ahmed N, Dobler D, Dean M, Thornalley P (2005) Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity. J Biol Chem 280:5724-5732 (Pubitemid 40280052)
44. Aliaga A, Garrido C, Leyton P, Diaz G, Gomez-Jeria J, Aguayo T, Clavijo E, Campos-Vallette M, Sanchez-Cortes S (2010) SERS and theoretical studies of arginine. Spectrochim Acta A 76:458-463
45. Bos O, Remijn J, Fischer M, Wilting J, Janssen L (1988) Location and characterization of the warfarin binding site of human serum albumin A comparative study of two large fragments. Biochem Pharmacol 37:3905-3909
46. Kosa T, Maruyama T, Otagiri M (1997) Species differences of serum albumins: I. Drug binding sites. Pharm Res 14:1607-1612 (Pubitemid 28009214)
47. Watanabe H, Kragh-Hansen U, Tanase S, Nakajou K, Mitarai M, Iwao Y, Maruyama T, Otagiri M (2001) Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants. Biochem J 357:269-274 (Pubitemid 32642926)
48. Petitpas I, Bhattacharya A, Twine S, East M, Curry S (2001) Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I. J Biol Chem 276:22804-22809
49. Carter D, Ho J (1994) Structure of serum albumin. Adv Protein Chem 45:153-203 (Pubitemid 24139888)
50. He X, Carter D (1992) Atomic structure and chemistry of human serum albumin. Nature 358:209-215
51. Pillai Z, Kamat P (2004) What factors control the size and shape of silver nanoparticles in the citrate ion reduction method? J Phys Chem B 108:945-951
52. Gubler CJ, Lahey M, Cartwright G, Wintrobe M (1953) Studies on copper metabolism. IX. The transportation of copper in blood. J Clin Invest 32:405-414
53. Peters T, Blumenstock F (1967) Copper binding properties of bovine serum albumin and its amino-terminal peptide fragment. J Biol Chem 242:1574-1578
54. Bal W, Christodoulou J, Sadler P, Tucker A (1998) Multi-metal binding site of serum albumin. J Inorg Biochem 70:33-39 (Pubitemid 28340621)
55. 2+. Eur J Biochem 220:193-200
56. Zgirski A, Frieden E (1990) Binding of Cu(II) to non-prosthetic sites in ceruloplasmin and bovine serum albumin. J Inorg Biochem 39:137-148 (Pubitemid 20202650)
57. Pifat G, Brnjas-Kraljević J, Jürgens G, Herak-Kramberger C, Herak J (1992) Chemical modification of low-density lipoprotein enhances the number of binding sites for divalent cations. Chem Phys Lipids 63:159-167 (Pubitemid 23052202)
58. Roland A, Patterson R, Leake D (2001) Measurement of copper-binding sites on low density lipoprotein. Arterioscler Thromb Vasc Biol 21:594-602 (Pubitemid 32323394)
59. Tainer J, Getzoff E, Richardson J, Richardson D (1983) Structure and mechanism of copper, zinc superoxide dismutase. Nature 306:284-287 (Pubitemid 14232362)
60. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S (1996) The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272:1136-1144