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.
de Vries
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Laboratory of Physical Chemistry and Colloid Science, Department of Agrotechnology and Food Sciences, Wageningen University, P.O. Box 8038, 6700 EK Wageningen, The Netherlands.
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