Solution Behavior and Interaction of Pepsin with Carnitine Based Cationic Surfactant: Fluorescence, Circular Dichroism, and Calorimetric Studies

Journal of Physical Chemistry B

Volumn 119, Issue 39, 2015, Pages 12632-12643

  Ghosh, Subhajit ^a   Dolai, Subhrajyoti ^a   Patra, Trilochan ^a   Dey, Joykrishna ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BINS; BIOLOGICAL MATERIALS; CALORIMETRY; CATIONIC SURFACTANTS; CHLORINE COMPOUNDS; DENATURATION; DICHROISM; DYES; FLUORESCENCE; PROTEINS; SURFACE ACTIVE AGENTS; THERMODYNAMICS;

BINDING AFFINITIES; CIRCULAR DICHROISM SPECTRA; CONFORMATIONAL CHANGE; FLUORESCENCE PROBES; ISOTHERMAL TITRATION CALORIMETRY; LOW CONCENTRATIONS; SOLUTION BEHAVIOR; STERIC INTERACTIONS;

ALKALINITY;

CARNITINE; CATION; PEPSIN A; SOLUTION AND SOLUBILITY; SURFACTANT;

CALORIMETRY; CHEMISTRY; CIRCULAR DICHROISM; PH; PROCEDURES; SOLUTION AND SOLUBILITY; SPECTROFLUOROMETRY; THERMODYNAMICS;

CALORIMETRY; CARNITINE; CATIONS; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; PEPSIN A; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; SURFACE-ACTIVE AGENTS; THERMODYNAMICS;

EID: 84942856194     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.5b07072     Document Type: Article

References (51)

1. Liu, C. L.; Kamei, D. T.; King, J. A.; Wang, D. I. C.; Blankschtein, D. Separation of proteins and viruses using two-phase aqueous micellar systems J. Chromatogr., Biomed. Appl. 1998, 711, 127-138 10.1016/S0378-4347(98)00013-9
2. Saitoh, T.; Tani, H.; Kamidate, T.; Watanabe, H. Phase separation in aqueous micellar solutions of nonionic surfactants for protein separation TrAC, Trends Anal. Chem. 1995, 14, 213-217 10.1016/0165-9936(95)91372-Y
3. Reynolds, J. A.; Tanford, C. Chemistry and metabolism of macromolecules J. Biol. Chem. 1970, 245, 5161-5165
4. Tanford, C. Hydrophobic free energy, micelle formation and the association of proteins with amphiphiles J. Mol. Biol. 1972, 67, 59-74 10.1016/0022-2836(72)90386-5
5. Shirahama, K.; Tsujii, K.; Takagi, T. Free-boundary electrophoresis of sodium dodecyl sulfate-protein polypeptide complexes with special reference to SDS-polyacrylamide gel electrophoresis J. Biochem. (Tokyo) 1974, 75, 309-314
6. Jones, M. N.; Manley, P. Binding of n-alkyl sulphates to lysozyme in aqueous solution J. Chem. Soc., Faraday Trans. 1 1979, 75, 1736-1744 10.1039/f19797501736
7. Griffiths, P. C.; Roe, J. A.; Bales, B. L.; Pitt, A. R.; Howe, A. M. Fluorescence probe studies of gelatin-sodium dodecyl sulfate interactions Langmuir 2000, 16, 8248-8254 10.1021/la0001833
8. Otzen, D. Protein-surfactant interactions: A tale of many states Biochim. Biophys. Acta, Proteins Proteomics 2011, 1814, 562-591 10.1016/j.bbapap.2011.03.003
9. Randolph, T. W.; Jones, L. S. Surfactant-protein interactions. In Rational design of stable protein formulations; Carpenter, J. F.; Manning, M., Eds.; Kluwer Academic/Plenum Publishers: New York, 2002; pp 159-175.
10. Jones, M. N. Protein-surfactant interactions. In Surface activity of proteins; Magdassi, S., Ed.; Marcel Dekker: New York, 1996; pp 237-284.
11. Tanford, C. The hydrophobic effect. Formation of micelles and biological membranes, 2 nd ed.; Wiley & Sons: New York, 1980.
12. Steinhardt, J. The nature of specific and non-specific interactions of detergents with proteins: Complexing and unfolding. In Protein-Ligand Interactions; Sund, H.; Blauer, G., Eds.; Walter de Gruyter, University of Konstanz: Berlin, Germany, 1975; pp 412-426.
13. Nieto-Ortega, B.; Hierrezuelo, J.; Ruiz, C. C.; Navarrete, J. T. L.; Casado, J.; Ramírez, F. J. Unfolding pathway of a globular protein by surfactants monitored with raman optical activity J. Phys. Chem. Lett. 2014, 5, 8-13 10.1021/jz402291s
14. De, D.; Santra, K.; Datta, A. Prototropism of [2,2′-Bipyridyl]-3,3′-diol in albumin-SDS aggregates J. Phys. Chem. B 2012, 116, 11466-11472 10.1021/jp306027h
15. Stenstam, A.; Khan, A.; Wennerstrom, H. The lysozyme-dodecyl sulfate system. an example of protein-surfactant aggregation Langmuir 2001, 17, 7513-7520 10.1021/la011096t
16. Liu, W.; Guo, X.; Guo, R. The interaction between hemoglobin and two surfactants with different charges Int. J. Biol. Macromol. 2007, 41, 548-557 10.1016/j.ijbiomac.2007.07.006
17. Tofani, L.; Feis, A.; Snoke, R. E.; Berti, D.; Baglioni, P.; Smulevich, G. Spectroscopic and interfacial properties of myoglobin/surfactant complexes Biophys. J. 2004, 87, 1186-1195 10.1529/biophysj.104.041731
18. Ghosh, S.; Banerjee, A. A multitechnique approach in protein/surfactant interaction study: physicochemical aspects of sodium dodecyl sulfate in the presence of trypsin in aqueous medium Biomacromolecules 2002, 3, 9-16 10.1021/bm005644d
19. Ghosh, S. Interaction of sodium dodecyl sulfate (SDS) with two globular proteins (trypsin and papain) in aqueous medium J. Surf. Sci. Technol. 2003, 19, 167-181
20. Ghosh, S. Physicochemical and conformational studies of papain/sodium dodecyl sulfate system in aqueous medium Colloids Surf., A 2005, 264, 6-161 10.1016/j.colsurfa.2005.02.032
21. Nielsen, A. D.; Borch, K.; Westh, P. Thermochemistry of the specific binding of C12 surfactants to bovine serum albumin Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. 2000, 1479, 321-331 10.1016/S0167-4838(00)00012-1
22. Otzen, D. E.; Sehgal, P.; Westh, P. α-Lactalbumin is unfolded by all classes of detergents but with different mechanisms J. Colloid Interface Sci. 2009, 329, 273-283 10.1016/j.jcis.2008.10.021
23. Lundahl, P.; Greijer, E.; Sandberg, M.; Cardell, S.; Eriksson, K.-O. A model for ionic and hydrophobic interactions and hydrogen-bonding in sodium dodecyl sulfate-protein complexes Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. 1986, 873, 20-26 10.1016/0167-4838(86)90184-6
24. Gull, N.; Chodankar, S.; Aswal, V. K.; Sen, P.; Khan, R. H.; Kabir-ud-Din Spectroscopic studies on the interaction of cationic surfactants with bovine serum albumin Colloids Surf., B 2009, 69, 122-128 10.1016/j.colsurfb.2008.11.009
25. Sun, C.; Yang, J.; Wu, X.; Huang, X.; Wang, F.; Liu, S. Unfolding and refolding of bovine serum albumin induced by cetylpyridinium bromide Biophys. J. 2005, 88, 3518-3524 10.1529/biophysj.104.051516
26. Madaeni, S. S.; Rostami, E. Spectroscopic investigation of the interaction of BSA with cationic surfactants Chem. Eng. Technol. 2008, 31, 1265-1271 10.1002/ceat.200700496
27. Kun, R.; Kis, L.; Dékány, I. Hydrophobization of bovine serum albumin with cationic surfactants with different hydrophobic chain length Colloids Surf., B 2010, 79, 61-68 10.1016/j.colsurfb.2010.03.028
28. Gospodarczyk, W.; Szutkowski, K.; Kozak, M. Interaction of bovine serum albumin (BSA) with novel gemini surfactants studied by synchrotron radiation scattering (SR-SAXS), circular dichroism (CD), and nuclear magnetic resonance (NMR) J. Phys. Chem. B 2014, 118, 8652-8661 10.1021/jp5047485
29. Wang, Y.; Jiang, X.; Zhou, L.; Yang, L.; Xia, G.; Chen, Z.; Duan, M. Synthesis and binding with BSA of a new gemini surfactant Colloids Surf., A 2013, 436, 1159-1169 10.1016/j.colsurfa.2013.08.045
30. Tai, S.; Liu, X.; Chen, W.; Gao, Z.; Niu, F. Spectroscopic studies on the interactions of bovine serum albumin with alkyl sulfate gemini surfactants Colloids Surf., A 2014, 441, 532-538 10.1016/j.colsurfa.2013.10.003
31. Mir, M. U. H.; Maurya, J. K.; Ali, S.; Ubaid-ullah, S.; Khan, A. B.; Patel, R. Molecular interaction of cationic gemini surfactant with bovine serum albumin: A spectroscopic and molecular docking study Process Biochem. 2014, 49, 623-630 10.1016/j.procbio.2014.01.020
32. Tang, J.; Sepulveda, P.; Marciniszyn, J., JR; Chen, K. C. S.; Huang, W.-Y.; Tao, N.; Liu, D.; Lanier, J. P. Amino-acid sequence of porcine pepsin Proc. Natl. Acad. Sci. U. S. A. 1973, 70, 3437-3439 10.1073/pnas.70.12.3437
33. Pande, M.; Kumari, N. K. P.; Dubey, V. K.; Tripathi, P.; Jagannadham, M. V. Stability and unfolding studies on alkaline denatured state (Ip) of pepsin Process Biochem. 2009, 44, 906-911 10.1016/j.procbio.2009.04.016
34. Zhang, H.; Cao, J.; Fei, Z.; Wang, Y. Investigation on the interaction behavior between bisphenol A and pepsin by spectral and docking studies J. Mol. Struct. 2012, 1021, 34-39 10.1016/j.molstruc.2012.04.072
35. Huang, Y.; Yan, J.; Liu, B.; Yu, Z.; Cao, X.; Tang, Y.; Zi, Y. Investigation on interaction of prulifloxacin with pepsin: A spectroscopic analysis Spectrochim. Acta, Part A 2010, 75, 1024 10.1016/j.saa.2009.12.044
36. Chakraborty, T.; Chakraborty, I.; Moulik, S. P.; Ghosh, S. Physicochemical studies on pepsin-CTAB interaction: Energetics and structural changes J. Phys. Chem. B 2007, 111, 2736-2746 10.1021/jp066051l
37. Boeris, V.; Micheletto, Y.; Lionzo, M.; Pesce da Silveira, N.; Picó, G. Interaction behavior between chitosan and pepsin Carbohydr. Polym. 2011, 84, 459-464 10.1016/j.carbpol.2010.12.008
38. Patra, T.; Ghosh, S.; Dey, J. Cationic vesicles of a carnitine-derived single-tailed surfactant: Physicochemical characterization and evaluation of in vitro gene transfection efficiency J. Colloid Interface Sci. 2014, 436, 138-145 10.1016/j.jcis.2014.08.049
39. Lakowicz, J. R. Principles of fluorescence spectroscopy; Plenum Press: New York, 1983.
40. Campos, L. A.; Sancho, J. Interaction behavior between chitosan and pepsin FEBS Lett. 2003, 538, 89-95 10.1016/S0014-5793(03)00152-2
41. Kim, S. H.; Kinsella, J. E. Surface active properties of proteins: Effects of progressive succinylation on film properties and foamStability of glycinin J. Food Sci. 1987, 52, 1341-1343 10.1111/j.1365-2621.1987.tb14077.x
42. Herriott, R. M. Pepsinogen and pepsin J. Gen. Physiol. 1962, 45, 57-76 10.1085/jgp.45.4.57
43. Privalov, P. L.; Mateo, P. L.; Khechinashvili, N. N.; Stepanov, V. M.; Revina, L. P. Comparative thermodynamic study of pepsinogen and pepsin structure J. Mol. Biol. 1981, 152, 445-464 10.1016/0022-2836(81)90253-9
44. Surewicz, W. K.; Mantsch, H. H.; Chapman, D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment Biochemistry 1993, 32, 389-394 10.1021/bi00053a001
45. Ghosh, S.; Dolai, S.; Dey, J. Amyloid fibril formation by pepsin in neutral pH at room temperature Soft Matter 2013, 9, 11457-11460 10.1039/c3sm52410h
46. Zhang, Y.-Z.; Zhou, B.; Zhang, X.-P.; Huang, P.; Li, C.-H.; Liu, Y. Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods J. Hazard. Mater. 2009, 163, 1345-1352 10.1016/j.jhazmat.2008.07.132
47. Gelamo, E. L.; Silva, C. H. T. P.; Imasato, H.; Tabak, M. Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: Spectroscopy and modeling Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. 2002, 1594, 84-99 10.1016/S0167-4838(01)00287-4
48. Gelamo, E. L.; Tabak, M. Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants Spectrochim. Acta, Part A 2000, 56, 2255-2271 10.1016/S1386-1425(00)00313-9
49. Ross, P. D.; Subramanian, S. Thermodynamics of protein association reactions: Forces contributing to stability Biochemistry 1981, 20, 3096-3102 10.1021/bi00514a017
50. Ghosh, S.; Dey, J. Binding of fatty acid amide amphiphiles to bovine serum albumin: Role of amide hydrogen bonding J. Phys. Chem. B 2015, 119, 7804-7815 10.1021/acs.jpcb.5b00965
51. Ghosh, S.; Dey, J. Interaction of bovine serum albumin with N-acyl amino acid based anionic surfactants: Effect of head-group hydrophobicity J. Colloid Interface Sci. 2015, 458, 284-292 10.1016/j.jcis.2015.07.064