Hostname: page-component-586b7cd67f-dsjbd Total loading time: 0 Render date: 2024-11-27T05:42:31.990Z Has data issue: false hasContentIssue false
  • English
  • Français

Assembly of Nanoparticles from Bioactive Peptides and Chitosan

Published online by Cambridge University Press:  10 February 2011

B. Hu ,
Q. R. Huang  and
X. X. Zeng
B. Hu
Affiliation:
Department of Food Science, Rutgers University, 65 Dudley Road, New Brunswick, New Jersey 08901, USA; College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, People’s Republic of China;
Q. R. Huang
Affiliation:
Department of Food Science, Rutgers University, 65 Dudley Road, New Brunswick, New Jersey 08901, USA;
X. X. Zeng
Affiliation:
College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, People’s Republic of China;
Get access

Abstract

Assembly of nanoparticles from bioactive peptides, caseinophosphopeptides (CPPs) and chitosan (CS) at physiological conditions and various CS/CPPs mass ratios have been systematically studied using a combination of turbidimetric titration, dynamic light scattering (DLS), electrophoretic mobility (zeta-potential) and transmission electron microscopy (TEM). Peptides, incorporated with CS forming nanoparticles, have already been prepared and identified using liquid chromatography-tandem mass spectrometry (LC-MS-MS). They are characteristic with different amount of clusters of phosphorylated seryl residues. At low salt concentration, an increase of CS/CPP mass ratio shifted the critical pHϕ1, which designated the formation of CS/CPP nanocomplexes, as well as pHmax, representing the neutralization of positive and negative charge to higher pH values. The peptide-polymer binding mechanism was analyzed according to the results of DLS, electrophoretic mobility, and TEM. First, negatively charged CPPs absorbed to positively charged CS molecular chain to form intrapolymer nanocomplexes saturated with CPPs (CPPNP). Then, the negatively charged CPPNP was bridged by added positively charged CS. Finally, novel nano-scaled spherical brushes were formed as additional CS molecule absorbed back to and bound the CPPNP. Phosphorylated groups in the CPPs might be the dominant sites for interaction with –NH3+ on the CS molecular chain.

Keywords

transmission electron microscopy (TEM)nanostructureself-assembly
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1312: Symposium HH/II/JJ – Polymer-Based Materials and Composites—Synthesis, Assembly and Applications , 2011 , mrsf10-1312-jj02-02
Copyright
Copyright © Materials Research Society 2011

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Caruso, F., Mohwald, H., Protein multilayer formation on colloids through a stepwise self-assembly technique. J. Am. Chem. Soc. 121, 6039 (1999).Google Scholar
2. Cooper, C. L., Dubin, P. L., Kayitmazer, A. B., Turksen, S., Polyelectrolyte–protein complexes. Curr. Opin. Colloid Interface Sci. 10, 52 (2005).Google Scholar
3. de Kruif, C. G., Weinbreck, F., de Vries, R., Complex coacervation of proteins and anionic polysaccharides, Curr. Opin. Colloid Interface Sci. 9, 340 (2004)Google Scholar
4. Burgess, D. J., “Complex coacervation: Microcapsule formation,” Macromolecular Complexes in Chemistry and Biology, Eds. Dubin, P. L., Bock, J., Davies, R. M., Schulz, D. N., Thies, C., (Springer–Verlag, 1994) pp. 285–300.Google Scholar
5. Shoichet, M. S., Polymer Scaffolds for Biomaterials Applications. Macromolecules 43, 581 (2010).Google Scholar
6. Mezzenga, R., Schurtenberger, P., Burbidge, A., Michel, M, Understanding foods as soft materials. Nat. Mater. 4, 729 (2005).Google Scholar
7. Ubbink, J., Burbidge, A., Mezzenga, R., Food structure and functionality: a soft matter perspective. Soft Mater. 4, 1569 (2008).Google Scholar
8. Su, R. X., Qi, W., He, Z. M., Yuan, S. X., Zhang, Y. B., Pancreatic hydrolysis of bovine casein: Identification and release kinetics of phosphopeptides. Food Chem. 104, 276 (2007).Google Scholar
9. Erba, D., Ciappellano, S., Testolin, G., Effect of the ratio of casein phosphopeptides to calcium (w/w) on passive calcium transport in the distal small intestine of rats. Nutr. 18, 743 (2002).Google Scholar
10. Cross, K. J., Huq, N. L., Palamara, J. E., Perich, J. W., Reynolds, E. C., Physicochemical characterization of casein phosphopeptide-amorphous calcium phosphate nanocomplexes. J. Biol. Chem. 280, 15362 (2005).Google Scholar
11. Laparra, J. M., Alegria, A., Barbera, R., Farre, R, Antioxidant effect of casein phosphopeptides compared with fruit beverages supplemented with skimmed milk against H2O2-induced oxidative stress in Caco-2 cells. Food Res. Int. 41, 773 (2008).Google Scholar
12. Kampa, M., Loukas, S., Hatzoglou, A., Daminaki, A., Martin, P. M., Castanas, E., Opioid alkaloids and casomorphin peptides decrease the proliferation of prostatic cancer cell lines (LNCaP, PC3 and DU145) through a partial interaction with opioid receptors. Eur. J Pharmacol. 335, 255 (1997).Google Scholar
13. Hata, I., Higashiyama, S., Otani, H., Identification of a phosphopeptide in bovine -casein digest as a factor influencing proliferation and immunoglobulin production in lymphocyte cultures. J. Dairy Res. 65, 569 (1998).Google Scholar
14. Qi, L. F., Xu, Z. R., Jiang, X., Hu, C. H., Zou, X. F., Preparation and antibacterial activity of chitosan nanoparticles. Carbohydr. Res. 339, 2693 (2004).Google Scholar
15. Qi, L. F., Xu, Z. R., In vivo antitumor activity of chitosan nanoparticles. Bioorg. Med. Chem. Lett. 16, 4243 (2006).Google Scholar
16. Hu, B., Wang, S.S., Li, J., Meng, L.M., Zeng, X.X., Huang, Q.R., Assembly of Nanoparticles from Bioactive Peptides and Chitosan, ACS NANO (Submitted).Google Scholar
17. Xia, J. L., Dubin, P. L., Dautzenberg, H., Light scattering, electrophoresis, and turbidimetry studies of bovine serum albuminpoly(dimethyldiallylammonium chloride) complex. Langmuir 9, 2015 (1993).Google Scholar
18. Jiang, H. L., Zhu, K. J., Polyanion/gelatin complexes as pH sensitive gels for controlled protein release. J. Appl. Polym. Sci. 80, 1416 (2001).Google Scholar
19. Laos, k., Brownsey, G. J., Ring, S. G.,Interactions between furcellaran and the globular proteins bovine serum albumin and β-lactoglobulin. Carbohy. Polym. 67, 116 (2007).Google Scholar
20. Xia, J. L., Zhang, H. W., Rigsbee, D. R., Dubin, P. L., Shaikh, T, Structural elucidation of soluble polyelectrolyte-micelle complexes: intra-vs interpolymer association. Macromolecules 26, 2759 (1993).Google Scholar
21. Guzey, D., McClements, D. J., Formation, stability and properties of multilayer emulsions for application in the food industry. Adv. Colloid Interface Sci. 128–130, 227 (2006).Google Scholar
22. Wang, Y., Kimura, K., Huang, Q. R., Dubin, P. L., Jaeger, W., Effects of salt on polyelectrolyte– micelle coacervation. Macromolecules 32, 7128 (1999).Google Scholar