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Article Dans Une Revue International Journal of Biological Macromolecules Année : 2017

How the presence of a small molecule affects the complex coacervation between lactoferrin and β-lactoglobulin

Résumé

Heteroprotein complex coacervation corresponds to the formation of two liquid phases in equilibriuminduced by the interaction of two oppositely charged proteins. The more concentrated phase known ascoacervate phase, has attracted interest from several fields of science due to its potential applicationsfor example for encapsulation and delivery of bioactives. Prior such application, it is necessary to under-stand how the presence of small ligands affects the complex coacervation. In this work, we report onthe interaction of small ligand with individual proteins -lactoglobulin ( -LG) and lactoferrin (LF) andconsequences on their complex coacervation. ANS (8-Anilinonaphthalene-1-sulfonic acid), a fluorescentprobe, was used as model ligand. While ANS did not interact with -LG, it presented two sets of bindingsites with LF inducing its self-aggregation. Depending on its concentration, ANS modulated the shapeof -LG-LF macromolecular assembly. Coacervates were observed for ANS/LF molar ratio <25 againstamorphous aggregates for higher ANS/LF molar ratios. A maximum loading capacity of around 40 mg ofANS per gram of LF in the formed heteroprotein coacervates was reached

Dates et versions

hal-01510024 , version 1 (18-04-2017)

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Paternité - Partage selon les Conditions Initiales

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Guilherme M. Tavares, Thomas Croguennec, Pascaline Hamon, Antônio F. Carvalho, Said Bouhallab. How the presence of a small molecule affects the complex coacervation between lactoferrin and β-lactoglobulin. International Journal of Biological Macromolecules, 2017, 102, pp.192-199. ⟨10.1016/j.ijbiomac.2017.04.007⟩. ⟨hal-01510024⟩
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