Effects of surface charge distribution of proteins in their complexation with polyelectrolytes in an aqueous salt-free system

Langmuir

Volumn 16, Issue 7, 2000, Pages 3133-3140

  Takahashi, Daisuke ^a   Kubota, Yuichi ^a   Kokai, Kenji ^a   Izumi, Tsuyoshi ^a   Hirata, Mitsuo ^a   Kokufuta, Etsuo ^b  

^a NIHON UNIVERSITY   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION; AGGLOMERATION; COMPLEXATION; ENZYMES; ESTERIFICATION; HYDRODYNAMICS; MOLECULAR WEIGHT; PH; POLYELECTROLYTES; POTASSIUM COMPOUNDS; TITRATION; TURBIDITY;

POTASSIUM POLYVINYL ALCOHOL SULFATE; QUASI-ELASTIC LIGHT SCATTERING (QELS); STATIC LIGHT SCATTERING (SLS); TURBIDIMETRIC TITRATION;

PROTEINS;

EID: 0033901658     PISSN: 07437463     EISSN: None     Source Type: Journal    
DOI: 10.1021/la991108z     Document Type: Article

References (20)

1. Kokufuta, E. In Macromolecular Complexes in Chemistry and Biology; Dubin, P. L., Davis, R., Thies, C., Bock, J., Schulz, D., Eds.; Springer-Verlag: Heidelberg, 1993; Chapter 18.
2. Xia, J.; Dubin, P. L.; Ahmed, L. S.; Kokufuta, E. In Macro-ion Characterization: From Dilute Solutions to Complex Fluids; Schmitz, K. S., Ed.; American Chemical Society: Washington, DC, 1994; Chapter 17.
3. Kokufuta, E.; Shimizu, H.; Nakamura, I. Polym. Bull. 1980, 2, 157.
4. Kokufuta, E.; Shimizu, H.; Nakamura, I. Macromolecules 1980, 14, 1178.
5. Kokufuta, E.; Shimizu, H.; Nakamura, I. Macromolecules 1981, 15, 1618.
6. Kokufuta, E., Takahashi, K. Polymer 1990, 31, 1177.
7. Izumi, T.; Hirata, M.; Takahashi, K.; Kokufuta, E. J. Macromol. Sci., Pure Appl. Chem. 1994, A31, 39.
8. Kokufuta, E. Prog. Polym. Sci. 1992, 17, 647 and references therein.
9. Tsuboi, A.; Izumi, T.; Hirata, M.; Xia, J.; Dubin, P. L.; Kokufuta, E. Langmuir 1996, 12, 6295.
10. Prior to our report (ref 9) on the formation of an intrapolymer PPC in a salt-free system, it was known that intrapolymer PPCs are formed in a salt-containing system (Xia, J.; Dubin, P. L.; Dautzenberg, H. Langmuir 1993,9, 2015). On the other hand, our recent study has demonstrated that the complexation of protein with a "neutral" polymer such as poly(ethylene glycol) gives forth a very stable and water-soluble intrapolymer complex (Azegami, S.; Tsuboi, A.; Izumi, T.; Hirata, M.; Dubin, P. L.; Wang, B.; Kokufuta, E. Langmuir 1999, 15, 940).
11. Prior to our report (ref 9) on the formation of an intrapolymer PPC in a salt-free system, it was known that intrapolymer PPCs are formed in a salt-containing system (Xia, J.; Dubin, P. L.; Dautzenberg, H. Langmuir 1993,9, 2015). On the other hand, our recent study has demonstrated that the complexation of protein with a "neutral" polymer such as poly(ethylene glycol) gives forth a very stable and water-soluble intrapolymer complex (Azegami, S.; Tsuboi, A.; Izumi, T.; Hirata, M.; Dubin, P. L.; Wang, B.; Kokufuta, E. Langmuir 1999, 15, 940).
12. We obtained information about both proteins from the Protein Data Bank, Oct 1996, Release No. 78, Brookhaven National Laboratory, Upton, NY. For details of these data bank, see: Abola, E. E.; Manning, N. O.; Prilusky, J.; Stampf, D. R.; Sussman, J. L. J. Res. Natl. Inst. Stand. Technol. 1996, 101, 231.
13. (a) Park, J. M., Muhoberac, B. B., Dubin, P. L., Xia, J. Macromolecules 1992, 25, 290.
14. (b)Mattison, K. W.; Dubin, P. L.; Brittain, I. J. Phys. Chem. B 1998, 102, 3830.
15. Takahashi, A., Nagasawa, M., Kagawa, T. Kougyo Kagaku Zasshi (an article published by Chemical Society of Japan) 1958, 61, 1614 (in Japanese).
16. g against molecular weight for PVA in pure water gave the slope of 0.56 (see: Wang, B.; Mukataka, S.; Kodama, M.; Kokufuta, E. Langmuir 1997, 13, 6108). Taking this into account, we may say that the polyion charges are fully eliminated in 0.2 M NaCl used as the solvent for our SLS and QELS measurements.
17. A relation between turbidity (τ) and absorbance (A) is given by τ = 2.3A/l, where l is cell length.
18. e = 0.92 from the length of the C-C bond (1.5 Å). On the other hand, a hydrodynamic diameter is about 40 Å for both proteins (see Table 2 of ref 9). Thus, from Figure 4 it is found that several charges on Lyz are located at an unfavorable spacing which is not complementary to the spacing between the polymer-bound anions, for example, the spacing between positions 73 and 97 as well as between positions 73 and 112. In contrast, most of the charges on RNase are located at favorable positions at which some chance of forming ion pairs with a polyanion is expectable, with a few exceptions (e.g., the spacing between positions 39 and 91).
19. 1.
20. Hydrodynamic theory (Konishi, T.; Yoshizaki, T.; Yamakawa, H. Macromolecules 1991, 24, 5614) shows that p changes from infinity to 0.775 when the polymer structure changes from a long rod to a sphere, with values from 1.3 to 1.5 for random coils.