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Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties.

ABSTRACT: Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding properties of native β-lg (localization of binding sites, stoichiometry, and affinity) and the way the interaction affects the biological properties of the protein and the ligand. The binding properties of non-native aggregated forms of β-lg that are classically generated during industrial processing are also related. Structural changes modify the stoichiometry and the affinity of β-lg for fatty acids and consequently the biological functions of the complex. Finally, the fatty acid-binding properties of other whey proteins (α-lactalbumin, bovine serum albumin) and some biological properties of the complexes are also addressed. These proteins affect β-lg/fatty acids complex in whey given their competition with β-lg for fatty acids.

SUBMITTER: Le Maux S

PROVIDER: S-EPMC4121524 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties.

Le Maux Solène S Bouhallab Saïd S Giblin Linda L Brodkorb André A Croguennec Thomas T

Dairy science & technology 20140227

Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding properties of native β-lg (localization of binding sites, stoichiometry, and affin ...[more]

PMID: 25110551

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Project description:BackgroundFatty acid (FA) binding proteins (FABPs) of helminths are implicated in acquisition and utilization of host-derived hydrophobic substances, as well as in signaling and cellular interactions. We previously demonstrated that secretory hydrophobic ligand binding proteins (HLBPs) of Taenia solium metacestode (TsM), a causative agent of neurocysticercosis (NC), shuttle FAs in the surrounding host tissues and inwardly transport the FAs across the parasite syncytial membrane. However, the protein molecules responsible for the intracellular trafficking and assimilation of FAs have remained elusive.Methodology/principal findingsWe isolated two novel TsMFABP genes (TsMFABP1 and TsMFABP2), which encoded 133- and 136-amino acid polypeptides with predicted molecular masses of 14.3 and 14.8 kDa, respectively. They shared 45% sequence identity with each other and 15-95% with other related-members. Homology modeling demonstrated a characteristic ?-barrel composed of 10 anti-parallel ?-strands and two ?-helices. TsMFABP2 harbored two additional loops between ?-strands two and three, and ?-strands six and seven, respectively. TsMFABP1 was secreted into cyst fluid and surrounding environments, whereas TsMFABP2 was intracellularly confined. Partially purified native proteins migrated to 15 kDa with different isoelectric points of 9.2 (TsMFABP1) and 8.4 (TsMFABP2). Both native and recombinant proteins bound to 11-([5-dimethylaminonaphthalene-1-sulfonyl]amino)undecannoic acid, dansyl-DL-?-amino-caprylic acid, cis-parinaric acid and retinol, which were competitively inhibited by oleic acid. TsMFABP1 exhibited high affinity toward FA analogs. TsMFABPs showed weak binding activity to retinol, but TsMFABP2 showed relatively high affinity. Isolation of two distinct genes from an individual genome strongly suggested their paralogous nature. Abundant expression of TsMFABP1 and TsMFABP2 in the canal region of worm matched well with the histological distributions of lipids and retinol.Conclusions/significanceThe divergent biochemical properties, physiological roles and cellular distributions of the TsMFABPs might be one of the critical mechanisms compensating for inadequate de novo FA synthesis. These proteins might exert harmonized or independent roles on lipid assimilation and intracellular signaling. The specialized distribution of retinol in the canal region further implies that cells in this region might differentiate into diverse cell types during metamorphosis into an adult worm. Identification of bioactive systems pertinent to parasitic homeostasis may provide a valuable target for function-related drug design.

Project description:The removal of heavy metals from wastewater remains a challenge due to the limitations of current remediation methods. This study aims to develop multicomponent composites as inexpensive and environmentally friendly sorbents with enhanced capture of cadmium (Cd) and lead (Pb). The composites are based on calcium montmorillonite (CM) and activated carbon (AC) because of their proven effectiveness as sorbents for diverse toxins in environmental settings. In this study, we used a combination of computational and experimental methods to delineate that β-lactoglobulin enhances CM and AC binding and protection properties for Cd and Pb. Modeling and molecular dynamics simulations investigated the formation of material systems formed by CM and AC in complex with β-lactoglobulin and predicted their capacity to bind heavy metal ions at neutral pH conditions. Our simulations suggest that the enhanced binding properties of the material systems are attributed to the presence of several binding pockets formed by β-lactoglobulin for the two heavy metal ions. At neutral pH conditions, divalent Cd and Pb shared comparable binding propensities in all material systems, with the former being consistently higher than the latter. To validate the interactions depicted in simulations, two ecotoxicological models (L. minor and H. vulgaris) were exposed to Cd, Pb, and a mixture of the two. The inclusion of CM-lactoglobulin (β-lactoglobulin amended CM) and AC-lactoglobulin (β-lactoglobulin amended AC) at 0.05-0.2% efficiently and dose-dependently reduced the severe toxicity of metals and increased the growth parameters. This high efficacy of protection shown in the ecotoxicological models may result from the numerous possible interaction pockets of the β-lactoglobulin-amended materials depicted in simulations. The ecotoxicological models support the agreement with computations. This study serves as a proof of concept on how computations in tandem with experiments can be used in the design of multicomponent clay- and carbon-based sorbent amended systems with augmented functionalities for particular toxins.

Dataset Information

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties.

Publications

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties.

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