Inhibitory effect of copper nanoparticles on rosin modified surfactant induced aggregation of lysozyme

International Journal of Biological Macromolecules

Volumn 78, Issue , 2015, Pages 379-388

  Ishtikhar, Mohd ^a   Usmani, Salman Sadullah ^a   Gull, Nuzhat ^b   Badr, Gamal ^c   Mahmoud, Mohamed H ^d,e   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

^b Government Degree College for Women   (India)

^c Assiut University   (Egypt)

^d NATIONAL RESEARCH CENTRE   (Egypt)

^e KING SAUD UNIVERSITY   (Saudi Arabia)

Author keywords

Aggregation inhibition; Amorphous aggregate; Lysozyme; Nanoparticles; Rosin modified surfactant; Thermal aggregation

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; CONGO RED; COPPER NANOPARTICLE; DYE; ESTER DERIVATIVE; LYSOZYME; METAL NANOPARTICLE; NANOCOATING; NANOFILM; NANOMATERIAL; QUATERNARY AMINE OF ROSIN DIETHYLAMINOETHYL ESTER; ROSIN; SILVER NANOPARTICLE; SURFACTANT; THIOFLAVINE; UNCLASSIFIED DRUG; ZINC NANOPARTICLE; COPPER; HEN EGG LYSOZYME; PLANT RESIN; PROTEIN AGGREGATE;

ANALYTIC METHOD; ARTICLE; BINDING ASSAY; CIRCULAR DICHROISM; CONTROLLED RELEASE FORMULATION; ENERGY DISPERSIVE X RAY SPECTROSCOPY; LIGHT SCATTERING; MICROENCAPSULATION; NONHUMAN; PH MEASUREMENT; PROTEIN AGGREGATION; RAYLEIGH LIGHT SCATTERING; SCANNING ELECTRON MICROSCOPY; SUSTAINED RELEASE PREPARATION; TEMPERATURE MEASUREMENT; TURBIDITY; ANIMAL; CHEMISTRY; DRUG EFFECTS; METABOLISM;

ANIMALS; CIRCULAR DICHROISM; CONGO RED; COPPER; METAL NANOPARTICLES; MICROSCOPY, ELECTRON, SCANNING; MURAMIDASE; PROTEIN AGGREGATES; RESINS, PLANT; SURFACE-ACTIVE AGENTS;

EID: 84928738153     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2015.03.069     Document Type: Article

References (78)

1. Chiti F., Stefani M., Taddei N., Ramponi G., Dobson C.M. Nature 2003, 424:805-808.
2. Vetri V., Canale C., Relini A., Librizzi F., Militello V., Gliozzi A., Leone M. Biophys. Chem. 2007, 125:184-190.
3. Dobson C.M. Nature 2003, 426:884-890.
4. Dubey K., Anand B.G., Temgire M.K., Kar K. Biochemistry 2014, 53:8001-8004.
5. Stefani M., Dobson C.M. J. Mol. Med. (Berl) 2003, 81:678-699.
6. Luheshi L.M., Crowther D.C., Dobson C.M. Curr. Opin. Chem. Biol. 2008, 12:25-31.
7. Uversky V.N. Curr. Protein Pept. Sci. 2008, 9:507-540.
8. Waters E.J., Alexander G., Muhlack R., Pocock K.F., Colby C., O'Neill B.K., Høj P.B., Jones P. Aust. J. Grape Wine Res. 2005, 11:215-225.
9. Zhang D., Li H., Wang J.B. Int. J. Biol. Macromol. 2015, 72:243-253.
10. Choudhary S., Kishore N. PLOS ONE 2014, 9:e104600.
11. Dong X.Y., Meng Y., Feng X.D., Sun Y. Biotechnol. Prog. 2010, 26:150-158.
12. Ghosh S., Pandey N.K., Bhattacharya S., Roy A., Nagy N.V., Dasgupta S. Int. J. Biol. Macromol. 2015, 76:1-9.
13. Pandey N.K., Ghosh S., Nagy N.V., Dasgupta S. J. Biomol. Struct. Dyn. 2014, 32:1366-1378.
14. Wawer J., Krakowiak J., Szocinski M., Lustig Z., Olszewski M., Szostak K. Int. J. Biol. Macromol. 2015, 70:214-221.
15. Loveday S.M., Su J., Rao M.A., Anema S.G., Singh H. Biomacromolecules 2011, 12:3780-3788.
16. Bhattacharya M., Jain N., Mukhopadhyay S. J. Phys. Chem. B 2011, 115:4195-4205.
17. Tougu V., Karafin A., Zovo K., Chung R.S., Howells C., West A.K., Palumaa P. J. Neurochem. 2009, 110:1784-1795.
18. Uversky V.N., Fink A.L. Biochim. Biophys. Acta 2004, 1698:131-153.
19. Sen P., Fatima S., Khan J.M., Khan R.H. Int. J. Biol. Macromol. 2009, 44:163-169.
20. Wang S.S., Hung Y.T., Wen W.S., Lin K.C., Chen G.Y. Biochim. Biophys. Acta 2011, 1811:301-313.
21. Li Y., Cao M., Wang Y. J. Phys. Chem. B 2006, 110:18040-18045.
22. Beneke C.E., Viljoen A.M., Hamman J.H. Molecules 2009, 14:2602-2620.
23. Wilbon P.A., Chu F., Tang C. Macromol. Rapid Commun. 2013, 34:8-37.
24. Coppen J.J.W., Hone G.A. Food and Agriculture Organization of the United Nations 1995.
25. Satturwar P.M., Fulzele S.V., Dorle A.K. AAPS PharmSciTech 2003, 4:E55.
26. Mandaogade P.M., Satturwar P.M., Fulzele S.V., Gogte B.B., Dorle A.K. React. Funct. Polym. 2002, 50:233-243.
27. Fulzele S.V., Satturwar P.M., Dorle A.K. Eur. J. Pharm. Sci. 2003, 20:53-61.
28. Gull N., Khan J.M., Ishtikhar M., Qadeer A., Khan R.A., Gul M., Khan R.H. J. Colloid Interface Sci. 2015, 439:170-176.
29. Pellenc D., Berry H., Gallet O. J. Colloid Interface Sci. 2006, 298:132-144.
30. Giehm L., Oliveira C.L., Christiansen G., Pedersen J.S., Otzen D.E. J. Mol. Biol. 2010, 401:115-133.
31. Otzen D.E. Curr. Protein Pept. Sci. 2010, 11:355-371.
32. Khan J.M., Qadeer A., Chaturvedi S.K., Ahmad E., Rehman S.A., Gourinath S., Khan R.H. PLoS ONE 2012, 7:e29694.
33. Wang S.S., Chen Y.T., Chou S.W. Biochim. Biophys. Acta 2005, 1741:307-313.
34. Yang F., Zhang M., Zhou B.R., Chen J., Liang Y. J. Mol. Biol. 2006, 362:821-834.
35. Hamill A.C., Lee C.T. J. Phys. Chem. B 2009, 113:6164-6172.
36. Wang S.S., Liu K.N., Han T.C. Biochim. Biophys. Acta 2010, 1802:519-530.
37. Bae S.Y., Kim S., Hwang H., Kim H.K., Yoon H.C., Kim J.H., Lee S., Kim T.D. Biochem. Biophys. Res. Commun. 2010, 400:531-536.
38. Jeng U.S., Lin T.L., Lin J.M., Ho D.L. Phys. B: Condens. Matter 2006, 386:865-867.
39. Yajuan Li M.C., Wang Y. J. Phys. Chem. B 2006, 110:18040-18045.
40. Bhogale A., Patel N., Mariam J., Dongre P.M., Miotello A., Kothari D.C. Colloids Surf. B: Biointerfaces 2014, 113:276-284.
41. Booth D.R., Sunde M., Bellotti V., Robinson C.V., Hutchinson W.L., Fraser P.E., Hawkins P.N., Dobson C.M., Radford S.E., Blake C.C., Pepys M.B. Nature 1997, 385:787-793.
42. Ratnaparkhi A., Muthu S.A., Shiriskar S.M., Pissurlenkar R.R., Choudhary S., Ahmad B. J. Biomol. Struct. Dyn. 2014, 1-14.
43. Trexler A.J., Nilsson M.R. Curr. Protein Pept. Sci. 2007, 8:537-557.
44. He J., Wang Y., Chang A.K., Xu L., Wang N., Chong X., Li H., Zhang B., Jones G.W., Song Y. J. Agric. Food Chem. 2014, 62:9442-9449.
45. Ravi V.K., Swain T., Chandra N., Swaminathan R. PLOS ONE 2014, 9:e87256.
46. Swaminathan R., Ravi V.K., Kumar S., Kumar M.V., Chandra N. Adv. Protein Chem. Struct. Biol. 2011, 84:63-111.
47. Naiki H., Gejyo F. Methods Enzymol. 1999, 309:305-318.
48. Atta A.M., El-Mahdy G.A., Dyab A.K.F., Allohedan H.A. Int. J. Electrochem. Sci. 2013, 8:9629-9643.
49. Wilbon P.A., Zheng Y., Yao K., Tang C. Macromolecules 2010, 43:8747-8754.
50. Khan J.M., Chaturvedi S.K., Rahman S.K., Ishtikhar M., Qadeer A., Ahmad E., Khan R.H. Soft Matter 2014, 10:2591-2599.
51. Ishtikhar M., Rabbani G., Khan R.H. Colloids Surf. B: Biointerfaces 2014, 123:469-477.
52. Qadeer A., Rabbani G., Zaidi N., Ahmad E., Khan J.M., Khan R.H. PLoS ONE 2012, 7:e50633.
53. Ishtikhar M., Khan S., Badr G., Osama A.M., Khan R.H. Mol. Biosyst. 2014, 10:2954-2964.
54. Chen Y.H., Yang J.T., Martinez H.M. Biochemistry 1972, 11:4120-4131.
55. Mir M.A., Khan J.M., Khan R.H., Dar A.A., Rather G.M. J. Phys. Chem. B 2012, 116:5711-5718.
56. Bourgault S., Solomon J.P., Reixach N., Kelly J.W. Biochemistry 2011, 50:1001-1015.
57. Ghosh N., Mondal R., Mukherjee S. Langmuir 2015, 31:1095-1104.
58. Ishtikhar M., Rabbani G., Khan S., Khan R.H. RSC Adv. 2014, 10.1039/C1034RA09892G.
59. Hawe A., Sutter M., Jiskoot W. Pharm. Res. 2008, 25:1487-1499.
60. Ahmad A., Muzaffar M., Ingram V.M. Biochim. Biophys. Acta 2009, 1794:1537-1548.
61. Sukenik S., Politi R., Ziserman L., Danino D., Friedler A., Harries D. PLoS ONE 2011, 6:e15608.
62. Khurana R., Coleman C., Ionescu-Zanetti C., Carter S.A., Krishna V., Grover R.K., Roy R., Singh S. J. Struct. Biol. 2005, 151:229-238.
63. Kumar S., Singh A.K., Krishnamoorthy G., Swaminathan R. J. Fluoresc. 2008, 18:1199-1205.
64. Gu Z., Zhu X., Ni S., Su Z., Zhou H.M. Int. J. Biochem. Cell Biol. 2004, 36:795-805.
65. Kundu B., Guptasarma P. Biochem. Biophys. Res. Commun. 2002, 293:572-577.
66. Khurana R., Uversky V.N., Nielsen L., Fink A.L. J. Biol. Chem. 2001, 276:22715-22721.
67. Arnaudov L.N., de Vries R. Biophys. J. 2005, 88:515-526.
68. Zhang D., Neumann O., Wang H., Yuwono V.M., Barhoumi A., Perham M., Hartgerink J.D., Wittung-Stafshede P., Halas N.J. Nano Lett. 2009, 9:666-671.
69. Yang M., Dutta C., Tiwari A. J. Phys. Chem. B 2015, 119:3969-3981.
70. Maiti M., Roy A., Roy S. Langmuir 2013, 29:13329-13338.
71. Hayes R., Imberti S., Warr G.G., Atkin R. Phys. Chem. Chem. Phys. 2011, 13:13544-13551.
72. Watanabe H., Tanase S., Nakajou K., Maruyama T., Kragh-Hansen U., Otagiri M. Biochem. J. 2000, 349(Pt 3):813-819.
73. Schmidt A.C., Storr B., Kummer N.A. Talanta 2011, 85:1118-1128.
74. Jaiswal S., McHale P., Duffy B. Colloids Surf. B: Biointerfaces 2012, 94:170-176.
75. Stranks S.D., Ecroyd H., Van Sluyter S., Waters E.J., Carver J.A., von Smekal L. Phys. Rev. E: Stat. Nonlinear Soft Matter Phys. 2009, 80:051907.
76. Rabbani G., Khan M.J., Ahmad A., Maskat M.Y., Khan R.H. Colloids Surf. B: Biointerfaces 2014, 123:96-105.
77. Golub E.E., Cheruka J., Boosz B., Davis C., Malamud D. Infect. Immun. 1985, 48:204-210.
78. Singh B.N., Rawat A.K., Khan W., Naqvi A.H., Singh B.R. PLOS ONE 2014, 9:e106937.