Monte Carlo simulations of flexible polyanions complexing with whey proteins at their isoelectric point.
Electrostatic complexation of flexible polyanions with the whey proteins alpha-lactalbumin and beta-lactoglobulin is studied using Monte Carlo simulations. The proteins are considered at their respective isoelectric points. Discrete charges on the model polyelectrolytes and proteins interact through Debye-Huckel potentials. Protein excluded volume is taken into account through a coarse-grained model of the protein shape. Consistent with experimental results, it is found that alpha-lactalbumin complexes much more strongly than beta-lactoglobulin. For alpha-lactalbumin, strong complexation is due to localized binding to a single large positive "charge patch," whereas for beta-lactoglobulin, weak complexation is due to diffuse binding to multiple smaller charge patches.
Laboratory of Physical Chemistry and Colloid Science, Department of Agrotechnology and Food Sciences, Wageningen University, P.O. Box 8038, 6700 EK Wageningen, The Netherlands.
R
R
de Vries
D000838:Anions; D001665:Binding Sites; D003198:Computer Simulation; D019281:Dimerization; D004548:Elasticity; D004563:Electrochemistry / Q000379:methods; D007768:Lactalbumin / Q000737:chemistry*; D007782:Lactoglobulins / Q000737:chemistry*; D008894:Milk Proteins / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D009010:Monte Carlo Method; D046912:Multiprotein Complexes / Q000737:chemistry*; D011485:Protein Binding
D000838:Anions; D007782:Lactoglobulins; D008894:Milk Proteins; D046912:Multiprotein Complexes; C024471:whey acidic proteins; D007768:Lactalbumin