Effects of conformational ordering on protein/polyelectrolyte electrostatic complexation: Ionic binding and chain stiffening

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Cao, Yiping ^a   Fang, Yapeng ^a   Nishinari, Katsuyoshi ^a   Phillips, Glyn O ^a  

^a HUBEI UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ANION; CARRAGEENAN; GELATIN; MONOVALENT CATION; POLYELECTROLYTE; POTASSIUM CHLORIDE; PROTEIN BINDING; QUATERNARY AMMONIUM DERIVATIVE; SOLUTION AND SOLUBILITY; TETRAMETHYLAMMONIUM;

BINDING SITE; CHEMISTRY; CONFORMATION; SOLUTION AND SOLUBILITY; STATIC ELECTRICITY; THERMODYNAMICS;

ANIONS; BINDING SITES; CARBOHYDRATE CONFORMATION; CARRAGEENAN; CATIONS, MONOVALENT; GELATIN; POLYELECTROLYTES; POTASSIUM CHLORIDE; PROTEIN BINDING; QUATERNARY AMMONIUM COMPOUNDS; SOLUTIONS; STATIC ELECTRICITY; THERMODYNAMICS;

EID: 84962860238     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep23739     Document Type: Article

References (46)

1. Felsenfeld, G., Groudine, M. Controlling the double helix. Nature 421, 448-453 (2003).
2. Stingele, J., Jentsch, S. DNA-protein crosslink repair. Nat. Rev. Mol. Cell Bio. 16, 455-460 (2015).
3. Kayitmazer, A. B., Seeman, D., Minsky, B. B., Dubin, P. L., Xu, Y. Protein-polyelectrolyte interactions. Soft Matter 9, 2553-2583 (2013).
4. Elzoghby, A. O., Samy, W. M., Elgindy, N. A. Protein-based nanocarriers as promising drug and gene delivery systems. J. Control. Release 161, 38-49 (2012).
5. Wu, B., Degner, B., McClements, D. J. Soft matter strategies for controlling food texture: formation of hydrogel particles by biopolymer complex coacervation. J. Phys. Condens. Mat. 26, 464104 (2014).
6. Yeo, Y., Bellas, E., Firestone, W., Langer, R., Kohane, D. S. Complex coacervates for thermally sensitive controlled release of flavor compounds. J. Agr. Food Chem. 53, 7518-7525 (2005).
7. Bosnea, L. A., Moschakis, T., Biliaderis, C. G. Complex coacervation as a novel microencapsulation technique to improve viability of probiotics under different stresses. Food Bioprocess Tech. 7, 2767-2781 (2014).
8. Li, X., Fang, Y., Al-Assaf, S., Phillips, G. O., Jiang, F. Complexation of bovine serum albumin and sugar beet pectin: stabilising oilin-water emulsions. J. Colloid Interface Sci. 388, 103-111 (2012).
9. Li, X. et al. Complexation of bovine serum albumin and sugar beet pectin: Structural transitions and phase diagram. Langmuir 28, 10164-10176 (2012).
10. Cao, Y. et al. Mapping the complex phase behaviors of aqueous mixtures of-carrageenan and type B gelatin. J. Phys. Chem. B 119, 9982-9992 (2015).
11. McClements, D. J. Non-covalent interactions between proteins and polysaccharides. Biotechnol. Adv. 24, 621-625 (2006).
12. Marcovitz, A., Levy, Y. Frustration in protein-DNA binding influences conformational switching and target search kinetics. Proc. Natl. Acad. Sci. USA 108, 17957-17962 (2011).
13. Ikeda, S., Nishinari, K. "Weak Gel"-type rheological properties of aqueous dispersions of nonaggregated-carrageenan helices. J. Agr. Food Chem. 49, 4436-4441 (2001).
14. Meinita, M. D. N. et al. Bioethanol production from the acid hydrolysate of the carrageenophyte Kappaphycus alvarezii (cottonii). J. Appl. Phycol. 24, 857-862 (2012).
15. Viebke, C., Borgstr, J., Carlsson, I., Piculell, L., Williams, P. A differential scanning calorimetry study of-carrageenan in the NaCl/NaI/CsI/CsCl systems and analysis by Poisson-Boltzmann calculations. Macromolecules 31, 1833-1841 (1998).
16. Grasdalen, H., Smidsroed, O. Iodide-specific formation of k-carrageenan single helixes. 127I NMR spectroscopic evidence for selective site binding of iodide anions in the ordered conformation. Macromolecules 14, 1842-1845 (1981).
17. Djabourov, M., Nishinari, K., Ross-Murphy, S. B. Physical gels from biological and synthetic polymers (first edition), 127-142 (Cambridge University Press, 2013).
18. Guo, L., Colby, R. H., Lusignan, C. P., Whitesides, T. H. Kinetics of triple helix formation in semidilute gelatin solutions. Macromolecules 36, 9999-10008 (2003).
19. Pelc, D., Marion, S., Požek, M., Basleti, M. Role of microscopic phase separation in gelation of aqueous gelatin solutions. Soft matter 10, 348-356 (2014).
20. Fang, Y., Li, L., Inoue, C., Lundin, L., Appelqvist, I. Associative and segregative phase separations of gelatin/-carrageenan aqueous mixtures. Langmuir 22, 9532-9537 (2006).
21. Vermeer, A. W., Norde, W. The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein. Biophys. J. 78, 394-404 (2000).
22. Bowman, W., Rubinstein, M., Tan, J. Polyelectrolyte-gelatin complexation: Light-scattering study. Macromolecules 30, 3262-3270 (1997).
23. Burgess, D. Practical analysis of complex coacervate systems. J. Colloid Interf. Sci. 140, 227-238 (1990).
24. Grasdalen, H., Smidsroed, O. 133Cs NMR in the sol-gel states of aqueous carrageenan. Selective site binding of cesium and potassium ions in k-carrageenan gels. Macromolecules 14, 229-231 (1981).
25. Schefer, L., Usov, I., Mezzenga, R. Anomalous stiffening and ion-induced coil-helix transition of carrageenans under monovalent salt conditions. Biomacromolecules 16, 985-991 (2015).
26. Bayley, S. T. X-ray and infrared studies on carrageenan. Biochimica et Biophysica Acta 17, 194-204 (1955).
27. Grinberg, V. Y. et al. Conformational energetics of interpolyelectrolyte complexation between-Carrageenan and poly (methylamino phosphazene) measured by high-sensitivity differential scanning calorimetry. Langmuir 27, 7714-7721 (2011).
28. Anderson, N., Campbell, J., Harding, M., Rees, D., Samuel, J. X-ray diffraction studies of polysaccharide sulphates: double helix models for-and-carrageenans. J. Mol. Biol. 45, 85-97 (1969).
29. Nerdal, W., Haugen, F., Knutsen, S., Grasdalen, H. Evidence for double helical kappa-carrageenan in aqueous LiI-solution and model for iodide binding. J. Biomol. Struct. Dynam. 10, 785-818 (1993).
30. Tanaka, F. Thermoreversible gelation driven by coil-to-helix transition of polymers. Macromolecules 36, 5392-5405 (2003).
31. Miller, S. E., Watkins, A. M., Kallenbach, N. R., Arora, P. S. Effects of side chains in helix nucleation differ from helix propagation. Proc. Natl. Acad. Sci. USA 111, 6636-6641 (2014).
32. Huang, J., MacKerell, A. D. Induction of peptide bond dipoles drives cooperative helix formation in the (AAQAA) 3 peptide. Biophys. J. 107, 991-997 (2014).
33. Boral, S., Bohidar, H. Effect of ionic strength on surface-selective patch binding-induced phase separation and coacervation in similarly charged gelatin-agar molecular systems. J. Phys. Chem. B 114, 12027-12035 (2010).
34. Kayitmazer, A., Seyrek, E., Dubin, P., Staggemeier, B. Influence of chain stiffness on the interaction of polyelectrolytes with oppositely charged micelles and proteins. J. Phys. Chem. B 107, 8158-8165 (2003).
35. Mattison, K. W., Dubin, P. L., Brittain, I. J. Complex formation between bovine serum albumin and strong polyelectrolytes: effect of polymer charge density. J. Phys. Chem. B 102, 3830-3836 (1998).
36. Yoo, J., Aksimentiev, A. Competitive binding of cations to duplex DNA revealed through molecular dynamics simulations. J. Phys. Chem. B 116, 12946-12954 (2012).
37. Cuenoud, B., Schepartz, A. Altered specificity of DNA-binding proteins with transition metal dimerization domains. Science 259, 510-513 (1993).
38. Morris, D. L. DNA-bound metal ions: recent developments. Biomol. Concepts 5, 397-407 (2014).
39. MacKerell, A. D., Nilsson, L. Molecular dynamics simulations of nucleic acid-protein complexes. Curr. Opin. Struc. Biol. 18, 194-199 (2008).
40. Driessen, R. P. et al. Effect of temperature on the intrinsic flexibility of DNA and its interaction with architectural proteins. Biochemistry 53, 6430-6438 (2014).
41. Capito, F., Skudas, R., Stanislawski, B., Kolmar, H. Polyelectrolyte-protein interaction at low ionic strength: required chain flexibility depending on protein average charge. Colloid Polym. Sci. 291, 1759-1769 (2013).
42. Tabata, Y., Hijikata, S., Ikada, Y. Enhanced vascularization and tissue granulation by basic fibroblast growth factor impregnated in gelatin hydrogels. J. Control. Release 31, 189-199 (1994).
43. Haug, I., Williams, M., Lundin, L., Smidsrod, O., Draget, K. Molecular interactions in, and rheological properties of, a mixed biopolymer system undergoing order/disorder transitions. Food Hydrocolloids 17, 439-444 (2003).
44. Ozawa, T. Kinetic analysis of derivative curves in thermal analysis. J. Therm. Anal. Calorim. 2, 301-324 (1970).
45. Mek, J. The applicability of Johnson-Mehl-Avrami model in the thermal analysis of the crystallization kinetics of glasses. Thermochim. Acta 267, 61-73 (1995).
46. Mckinney, R. M., Spillane, J. T., Pearce, G. W. Factors affecting the rate of reaction of fluorescein isothiocyanate with serum proteins. J. Immunol. 93, 232-242 (1964).