Specific binding of Minerals affects spontaneous co-assembly of globular proteins
2014
Bouhallab, Said | Miranda-Tavares, Guilherme | Hamon, Pascaline | Croguennec, Thomas
Formation of co-assembled structures by spontaneous association of oppositely charged proteins has increasing interest for the design of new supra-molecular structures. Research in our group seeks to understand the mechanisms that dictate the assembly of food proteins in order to control the properties (e.g. Shape, size, density] and functionalities [encapsulation,…] of generated supra-molecular structures. In this communication, we will show how do minerals affect the co-assembly of a globular metalloprotein with oppositely charged protein. This was illustrated by the co-assembly of lysozyme with native (holo) or calcium-depleted (apo) α-lactalbumin in one hand and of β-lactoglobulin with iron-loaded (holo) or iron-depleted (apo) lactoferrin in another hand. In both binary systems, the saturation of metallo-protein binding site(s) did not perturb the initial interaction step leading to hetero-proteins building blocks but subsequent aggregation steps of the building blocks were modified. Well-organized supra-molecular structures – nano- or microspheres- were generally favored with the apo-forms of proteins against amorphous unstructured aggregates with the holo-forms. The results are discussed on the basis of changes in protein conformation, flexibility and overall charges after metal removal. Throughout these examples, this study underlines that minerals are particularly useful for rationalizing the design of food protein based nano- or microparticles.
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