Dynamic and supramolecular organisation of α-lactalbumin/lysozyme microspheres: A microscopic study

Biophysical Chemistry

Volumn 146, Issue 1, 2010, Pages 30-35

  Nigen, Michaël ^a   Gaillard, Cédric ^b   Croguennec, Thomas ^a   Madec, Marie Noëlle ^a   Bouhallab, Saïd ^a  

^a AGROCAMPUS OUEST   (France)

^b INRA   (France)

Author keywords

lactalbumin; AFM; Assembly mechanism; CSLM; Lysozyme; TEM

Indexed keywords

ALPHA LACTALBUMIN; LYSOZYME; MICROSPHERE; NANOSPHERE;

ARTICLE; CONCENTRATION (PARAMETERS); INCUBATION TIME; MICROSCOPY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DETERMINATION; PROTEIN STRUCTURE; SUPRAMOLECULAR CHEMISTRY;

APOPROTEINS; LACTALBUMIN; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, CONFOCAL; MICROSCOPY, ELECTRON, SCANNING; MICROSCOPY, ELECTRON, TRANSMISSION; MICROSPHERES; MURAMIDASE; PROTEIN MULTIMERIZATION;

EID: 70449716897     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2009.10.001     Document Type: Article

References (29)

1. Goers J., Permyakov S.E., Permyakov E.A., Uversky V.N., and Fink A.L. Conformational prerequisites for -lactalbumin fibrillation. Biochemistry 41 (2002) 12546-12551
2. Graveland-Bikker J.F., and de Kruif C.G. Unique milk protein based nanotubes: food and nanotechnology meet. Trends Food Sci. Technol. 17 (2006) 196-203
3. Ipsen R., Otte J., and Qvist K.B. Molecular self-assembly of partially hydrolysed α-lactalbumin resulting in strong gels with a novel microstructure. J. Dairy Res. 68 (2001) 277-286
4. Krebs M.R.H., Devlin G.L., and Donald A.M. Protein particulates: another generic form of protein aggregation?. Biophys. J. 92 (2007) 1336-1342
5. Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
6. Krebs M.R.H., Bromley E.H.C., Rogers S.S., and Donald A.M. The mechanism of amyloid spherulite formation by bovine insulin. Biophys. J. 88 (2005) 2013-2021
7. Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., and Teplow D.B. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Nat. Acad. Sci. 93 (1996) 1125-1129
8. Leonil J., Henry G., Jouanneau D., Delage M.M., Forge V., and Putaux J.L. Kinetics of fibril formation of bovine -casein indicate a conformational rearrangement as a critical step in the process. J. Mol. Biol. 381 (2008) 1267-1280
9. Sanguansri P., and Augustin M.A. Nanoscale materials development - a food industry perspective. Trends Food Sci. Technol. 17 (2006) 547-556
10. Zhang S., Marini D.M., Hwang W., and Santoso S. Design of nanostructured biological materials through self-assembly of peptides and proteins. Curr. Opin. Chem. Biol. 6 (2002) 865-871
11. Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nat. Biotechnol. 21 (2003) 1171-1178
12. Viney C. Self-assembly as a route to fibrous materials: concepts, opportunities and challenges. Curr. Opin. Solid State Mater. Sci. 8 (2004) 95-101
13. Nigen M., Croguennec T., Renard D., and Bouhallab S. Temperature affects the supramolecular structures resulting from α-lactalbumin-lysozyme interaction. Biochemistry 46 (2007) 1248-1255
14. McKenzie H.A., and White F.H.J. Lysozyme and α-lactalbumin: structure, function, and interrelationships. Adv. Protein. Chem. 41 (1991) 173-315
15. Qasba P.K., and Kumar S. Molecular divergence of lysozymes and α-lactalbumin. Crit. Rev. Biochem. Mol. Biol. 32 (1997) 255-306
16. Greene L.H., Grobler J.A., Malinovskii V.A., Tian J., Acharya K.R., and Brew K. Stability, activity and flexibility in α-lactalbumin. Protein Eng. 12 (1999) 581-587
17. Iyer L.K., and Qasba P.K. Molecular dynamics simulation of α-lactalbumin and calcium binding c-type lysozyme. Protein Eng. 12 (1999) 129-139
18. Nigen M., Le Tilly V., Croguennec T., Drouin-Kucma D., and Bouhallab S. Molecular interaction between apo or holo-lactalbumin and lysozyme: formation of heterodimers as assessed by fluorescence measurements. Biochim. Biophys. Acta 1794 (2009) 709-715
19. Nigen M., Croguennec T., Madec M.N., and Bouhallab S. Apo-lactalbumin and lysozyme are co-localized in their subsequently formed spherical supramolecular assembly. FEBS J. 274 (2007) 6085-6093
20. Caussin F., Famelart M.H., Maubois J.L., and Bouhallab S. Mineral modulation of thermal aggregation and gelation of whey proteins: from β-lactoglobulin model system to whey protein isolate. Lait 83 (2003) 353-364
21. Mao S.Y. The Protein Protocols Handbook. In: Walker J.M. (Ed). Conjugation of fluorochromes to antibodies (2002), Humana Press, Totowa, New Jersey 351-354
22. Biesheuvel P.M., Lindhoud S., de Vries R., and Cohen Stuart M.A. Phase behavior of mixtures of oppositely charged nanoparticles: heterogeneous Poisson-Boltzmann cell model applied to lysozyme and succinylated lysozyme. Langmuir 22 (2006) 1291-1300
23. Biesheuvel P.M., Lindhoud S., Cohen Stuart M.A., and de Vries R. Phase behavior of mixtures of oppositely charged protein nanoparticles at asymmetric charge ratios. Phys. Rev. E 73 (2006) 041408
24. Nigen M., Croguennec T., and Bouhallab S. Formation and stability of -lactalbuminlysozyme spherical particles: involvement of electrostatic forces. Food Hydrocoll. 23 (2009) 510-518
25. Slotta U.K., Rammensee S., Gorb S., and Scheibel T. An engineered spider silk protein forms microspheres. Angew. Chem., Int. Ed. 47 (2008) 4592-4594
26. Lammel A., Schwab M., Slotta U., Winter G., and Scheibel T. Processing conditions for the formation of spider silk microspheres. ChemSusChem 1 (2008) 413-416
27. Gummel J., Boué F., Clemens D., and Cousin F. Finite size and inner structure controlled by electrostatic screening in globular complexes of proteins and polyelectrolytes. Soft Matter 4 (2008) 1653-1664
28. Bohr H., Kühle A., Sorensen A.H., and Bohr J. Hierarchical organization in aggregates of protein molecules. Z. Phys. D 40 (1997) 513-515
29. Zhong C., and Chu C.C. Acid polysaccharide-induced amorphous calcium carbonate (ACC) films: colloidal nanoparticle self-organization process. Langmuir 25 (2009) 3045-3049