Equilibrium studies of cellulase aggregates in presence of ascorbic and boric acid

International Journal of Biological Macromolecules

Volumn 52, Issue 1, 2013, Pages 286-295

  Iram, Afshin ^a   Amani, Samreen ^a   Furkan, Mohammad ^a   Naeem, Aabgeena ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Aggregates; Antioxidant; Cellulase; Molten globule state; Pro oxidant

Indexed keywords

ACRYLAMIDE; ASCORBIC ACID; BORIC ACID; CELLULASE; THIOFLAVINE; TRYPTOPHAN;

APOPTOSIS; ARTICLE; ASPERGILLUS NIGER; COMET ASSAY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME CONFORMATION; FLUORESCENCE; FOURIER TRANSFORM INFRARED PHOTOACOUSTIC SPECTROSCOPY; HYDRODYNAMICS; HYDROPHILICITY; LIGHT SCATTERING; NONHUMAN; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

EID: 84870222321     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2012.10.023     Document Type: Article

References (41)

1. Naeem A., Fazili N.A. Defective protein folding and aggregation as the basis of neurodegenerative diseases: the darker aspect of proteins. Cell Biochemistry and Biophysics 2011, 61:237-250.
2. Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Folding and Design 1998, 3:R9-R23.
3. Dong A.C., Prestrelski S.J., Allison S.D., Carpenter J.F. Infrared spectroscopic studies of lyophilization-induced and temperature-induced protein aggregation. Journal of Pharmaceutical Sciences 1995, 84:415-424.
4. Tartaglia G.G., Pawar A.P., Campioni S., Dobson C.M., Chiti F., Vendruscolo M. Prediction of aggregation-prone regions in structured proteins. Journal of Molecular Biology 2008, 380:425-436.
5. Armen R.S., DeMarco M.L., Alonso D.O.V., Daggett V. Pauling and Corey's pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proceedings of the National Academy of Sciences of the United States of America 2004, 101:11622-11627.
6. Iram A., Naeem A. Existence of different structural intermediates and aggregates on the folding pathway of ovalbumin. Journal of Fluorescence 2012, 22:47-57.
7. Iram A., Naeem A. Trifluoroethanol and acetonitrile induced formation of the molten globule states and aggregates of cellulase. International Journal of Biological Macromolecules 2012, 50:932-938.
8. Bhat M.K. Cellulases and related enzymes in biotechnology. Biotechnology Advances 2000, 18:355-383.
9. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the folin reagent. Journal of Biological Chemistry 1951, 193:266-275.
10. Dubois M., Gilles K., Hamilton J.K., Rebers P.A., Smith F. A colorimetric method for the determination of sugars. Nature 1951, 168:167-168.
11. Khan T.A., Amani S., Naeem A. Glycation promotes the formation of genotoxic aggregates in glucose oxidase. Amino Acids 2012, 43:1311-1322.
12. Stryer L. Fluorescence spectroscopy of proteins. Science 1968, 162:526-540.
13. Eftink M.R., Ghiron C.A. Fluorescence quenching studies with proteins. Analytical Biochemistry 1982, 114:199-227.
14. Hawe A., Sutter M., Jiskoot W. Extrinsic fluorescent dyes as tools for protein characterization. Pharmaceutical Research 2008, 25:1487-1499.
15. Greenfield N.J. Using circular dichroism spectra to estimate protein secondary structure. Nature Protocols 2007, 1:2876-2890.
16. Chung H.S., Khalil M., Tokmakoff A. Nonlinear infrared spectroscopy of protein conformational change during thermal unfolding. Journal of Physical Chemistry B 2004, 108:15332-15342.
17. Ferguson N., Berriman J., Petrovich M., Sharpe T.D., Finch J.T., Fersht A.R. Rapid amyloid fiber formation from the fast-folding WW domain FBP28. Proceedings of the National Academy of Sciences of the United States of America 2003, 100:9814-9819.
18. Klunk W.E., Jacob R.F., Mason R.P. Quantifying amyloid by Congo red spectral shift assay. Methods in Enzymology 1999, 309:285-305.
19. Coan K.E., Shoichet B.K. Stability and equilibria of promiscuous aggregates in high protein milieus. Molecular Biosystems 2007, 3:208-213.
20. Chaudhuri A., Haldar S., Chattopadhyay A. Organization and dynamics of tryptophans in the molten globule state of bovine α-lactalbumin utilizing wavelength-selective fluorescence approach: comparisons with native and denatured states. Biochemical and Biophysical Research Communications 2010, 394:1082-1086.
21. Caramelo J.J., Castro O.A., Alonso L.G., De Prat-Gay G., Parodi A.J. UDP-Glc: glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates. Proceedings of the National Academy of Sciences of the United States of America 2003, 100:86-91.
22. Muzammil S., Kumar Y., Tayyab S. Molten globule-like state of human serum albumin at low pH. European Journal of Biochemistry 1999, 266:26-32.
23. Matulis D., Baumann C.G., Bloomfield V.A., Lovrien R.E. 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 1999, 49:451-458.
24. Duy C., Fitter J. How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra. Biophysical Journal 2006, 90:3704-3711.
25. Plakoutsi G., Taddei N., Stefani M., Chiti F. Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursor for amyloid formation. Journal of Biological Chemistry 2004, 279:14111-14119.
26. Khademi S., Zhang D., Swanson S.M., Wartonberg A., Witte K., Meyer E.F. Determination of the structure of an endoglucanase from Aspergillus niger and its mode of inhibition by palladium chloride. Acta Crystallographica D 2002, 58:660-667.
27. Kendrick B.S., Cleland J.L., Lam X., Nquyen T., Randolph T.W., Manning M.C., Carpenter J.F. Aggregation of recombinant human interferon gamma: kinetics and structural transitions. Journal of Pharmaceutical Sciences 1998, 87:1069-1076.
28. Chapman A.L., Winterbourn C.C., Brennan S.O., Jordan T.W., Kettle A.J. Characterization of non-covalent oligomers of proteins treated with hypochlorous acid. Biochemical Journal 2003, 375:33-40.
29. Goormaghtigh E., Cabiaux V., Ruysschaert J.M. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. Sub-Cellular Biochemistry 1994, 23:405-450.
30. Naeem A., Khan T.A., Muzaffar M., Ahmad S., Saleemuddin M. A partially folded state of ovalbumin at low pH tends to aggregate. Cell Biochemistry and Biophysics 2011, 59:29-38.
31. Santiago S.P., Carvalho O., Adriano F., Domingues M.M., Carvalho J.W. Isoelectric point determination for Glossoscolex paulistus extracellular hemoglobin: oligomeric stability in acidic pH and relevance to protein-surfactant interactions. Langmuir 2010, 26:9794-9801.
32. Ghaouar N., Gharbi A. On the conformational changes of cellulase: dynamic light scattering study. Sensor Letters 2011, 9:2384-2387.
33. Khodadadi S., Pawlus S., Roh J.H., Garcia-Sakai V., Mamontov E., Sokolov A.P. The origin of the dynamic transition in proteins. Journal of Chemical Physics 2008, 128:195-206.
34. Vassar P.S., Culling C.F.A. Fluorescent stains with special reference to amyloid and connective tissues. Archives of Pathology 1959, 68:487-494.
35. Brorsson A.C., Bolognesi B., Tartaglia G.G., Shammas S.L., Fevrin G., Watson I., Lomas D.A., Chiti F., Vendruscolo M., Dobson C.M., Crowther D.C., Luheshi L.M. Intrinsic determinants of neurotoxic aggregate formation by the amyloid β-peptide. Biophysical Journal 2010, 98:1677-1684.
36. Cooper J.H. Selective amyloid staining as a function of amyloid composition and structure. Laboratory Investigation 1974, 31:232-238.
37. Cameron E., Pauling L. Supplemental ascorbate in the supportive treatment of cancer: reevaluation of prolongation of survival times in terminal human cancers. Proceedings of the National Academy of Sciences of the United States of America 1978, 75:4538-4542.
38. Riordan N.H., Riordan H.D., Meng X., Li Y., Jackson J.A. Intravenous ascorbate as tumor cytotoxic and tumor therapeutic agent. Medical Hypotheses 1995, 44:207-213.
39. Omaya T.S., Scala J.H., Jacob R.A. Plasma ascorbic acid in adult males: effects of depletions and supplementation. American Journal of Clinical Nutrition 1986, 44:257-264.
40. Padayatty S.J., Sun H., Wang Y., Riordan H.D., Hewit S., Katz A., Wesley R.A., Levine M. Vitamin C pharmacokinetics: implications for oral and intravenous use. Annals of Internal Medicine 2004, 140:533-538.
41. Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends in Biochemical Sciences 2001, 26:597-604.