How the presence of a small molecule affects the complex coacervation between lactoferrin and -lactoglobulin
Heteroprotein complex coacervation corresponds to the formation of two liquid phases in equilibrium induced by the interaction of two oppositely charged proteins. The more concentrated phase known as coacervate phase, has attracted interest from several fields of science due to its potential applica...
| Autores: | , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2017 |
| País: | Brasil |
| Institución: | Universidade Federal de Viçosa (UFV) |
| Repositorio: | LOCUS Repositório Institucional da UFV |
| Idioma: | inglés |
| OAI Identifier: | oai:locus.ufv.br:123456789/12645 |
| Acceso en línea: | http://dx.doi.org/10.1016/j.ijbiomac.2017.04.007 http://www.locus.ufv.br/handle/123456789/12645 |
| Access Level: | acceso abierto |
| Palabra clave: | Complex coacervation β-Lactoglobulin Lactoferrin ANS Binding ITC |
| Sumario: | Heteroprotein complex coacervation corresponds to the formation of two liquid phases in equilibrium induced by the interaction of two oppositely charged proteins. The more concentrated phase known as coacervate phase, has attracted interest from several fields of science due to its potential applications for example for encapsulation and delivery of bioactives. Prior such application, it is necessary to understand how the presence of small ligands affects the complex coacervation. In this work, we report on the interaction of small ligand with individual proteins β-lactoglobulin (β-LG) and lactoferrin (LF) and consequences on their complex coacervation. ANS (8-Anilinonaphthalene-1-sulfonic acid), a fluorescent probe, was used as model ligand. While ANS did not interact with β-LG, it presented two sets of binding sites with LF inducing its self-aggregation. Depending on its concentration, ANS modulated the shape of β-LG-LF macromolecular assembly. Coacervates were observed for ANS/LF molar ratio <25 against amorphous aggregates for higher ANS/LF molar ratios. A maximum loading capacity of around 40 mg of ANS per gram of LF in the formed heteroprotein coacervates was reached. |
|---|