Structure of bovine β-lactoglobulin (variant A) at very low ionic strength

Adams, J. F.; Anderson, Bill; Norris, Gillian E.; Creamer, Lawrence K.; Jameson, Geoffrey B.

doi:10.1016/j.jsb.2005.12.010

Cited by 57 publications

(35 citation statements)

References 41 publications

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“…Intrinsically, it could be ascribed to the exposure of more hydrophobic domains on the surface of β-lg than that of WPI and SPI, which was directly correlated with the probability of its adsorption and retention at the interface. 44 effect of oil-to-water ratio…”

Section: Resultsmentioning

confidence: 99%

Food protein-stabilized nanoemulsions as potential delivery systems for poorly water-soluble drugs: preparation, in vitro characterization, and pharmacokinetics in rats

He¹,

Tan²,

Tian³

et al. 2011

IJN

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Nanoemulsions stabilized by traditional emulsifiers raise toxicological concerns for long-term treatment. The present work investigates the potential of food proteins as safer stabilizers for nanoemulsions to deliver hydrophobic drugs. Nanoemulsions stabilized by food proteins (soybean protein isolate, whey protein isolate, β-lactoglobulin) were prepared by high-pressure homogenization. The toxicity of the nanoemulsions was tested in Caco-2 cells using the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazoliumbromide viability assay. In vivo absorption in rats was also evaluated. Food protein-stabilized nanoemulsions, with small particle size and good size distribution, exhibited better stability and biocompatibility compared with nanoemulsions stabilized by traditional emulsifiers. Moreover, β-lactoglobulin had a better emulsifying capacity and biocompatibility than the other two food proteins. The pancreatic degradation of the proteins accelerated drug release. It is concluded that an oil/water nanoemulsion system with good biocompatibility can be prepared by using food proteins as emulsifiers, allowing better and more rapid absorption of lipophilic drugs.

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Section: Resultsmentioning

confidence: 99%

Food protein-stabilized nanoemulsions as potential delivery systems for poorly water-soluble drugs: preparation, in vitro characterization, and pharmacokinetics in rats

He¹,

Tan²,

Tian³

et al. 2011

IJN

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“…The poses, obtained Figure 5 (see Table 4 for the energy ranking of the poses). This result suggests that the water molecules play a relevant role in the cL-BABP binding processes, differently from other proteins of the calycins superfamily, such as BLG, which has no water molecules inside its binding site, either in the apo-or in the holo-form (Qin et al, 1998;Adams et al, 2006). The absence of internal water molecules in BLG was reported not only in all crystallographic forms of BLG, but also in MD simulations (Eberini et al, 2004).…”

Section: Resultsmentioning

confidence: 88%

Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein

Ricchiuto¹,

Rocco²,

Gianazza³

et al. 2008

J of Molecular Recognition

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Chicken liver bile acid binding protein (cL-BABP) crystallizes with water molecules in its binding site. To obtain insights on the role of internal water, we performed two 100 ns molecular dynamics (MD) simulations in explicit solvent for cL-BABP, as apo form and as a complex with two molecules of cholic acid, and analyzed in detail the dynamics properties of all water molecules. The diffusion coefficients of the more persistent internal water molecules are significantly different from the bulk, but similar between the two protein forms. A different number of molecules and a different organization are observed for apo- and holo-cL-BABP. Most water molecules identified in the binding site of the apo-crystal diffuse to the bulk during the simulation. In contrast, almost all the internal waters of the holo-crystal maintain the same interactions with internal sidechains and ligands, which suggests they have a relevant role in protein-ligand molecular recognition. Only in the presence of these water molecules we were able to reproduce, by a classical molecular docking approach, the structure of the complex cL-BABP::cholic acid with a low ligand root mean square deviation (RMSD) with respect to its reference positioning. Literature data reported a conserved pattern of hydrogen bonds between a single water molecule and three amino acid residues of the binding site in a series of crystallized FABP. In cL-BABP, the interactions between this conserved water molecule and the three residues are present in the crystal of both apo- and holo-cL-BABP but are lost immediately after the start of molecular dynamics.

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“…The midpoint temperatures calculated for the wild-type ELG and BLG denaturations and for the Gyuba denaturation are 70.6 C, 74.2 and 64. 8 C, respectively, and the corresponding DH values at these temperatures are 252 6 3, 228 6 5, and 117 6 3 kJ/mol. Thus, the thermal stability of Gyuba is considerably lower compared with wild-type ELG and BLG, perhaps a consequence of structural mismatches between the loops and secondary structures in Gyuba (see Discussion).…”

Section: Thermal Denaturationmentioning

confidence: 94%

“…the EF-loop of Gyuba adopted the closed conformation, the BLG structures 1beb, 4 1bsq, 6 2akq, 8 and 3blg 5 (PDB accession numbers), for which the EFloops also adopted the closed conformation, were used for comparison. The superpositions revealed an obvious difference between the tertiary structures of BLG and Gyuba in the C-terminal regions, that is, the distances between each of the Cas for residues 153-157 of Gyuba and the each of the BLG structures were much larger than those for the remaining sequence in these proteins (Fig.…”

Section: Crystal Structure Of Gyubamentioning

confidence: 99%

“…2,3 However, the monomers retain their tertiary structures at acidic pH. Both crystal [4][5][6][7][8][9] and solution 10,11 structures of BLG show that the monomer contains nine b-strands (strands A-I), an ahelix, and three short 3 10 helices. Eight of the bstrands (A-H) form an up-and-down b-barrel, and the two I-strands form an intermolecular b-sheet containing four intermolecular hydrogen bonds.…”

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confidence: 99%

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Structure and stability of Gyuba, a β‐lactoglobulin chimera

Ohtomo¹,

Konuma²,

Utsunoiya³

et al. 2011

Protein Science

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b-lactoglobulin (LG) contains nine b-strands (strands A-I) and one a-helix. Strands A-H form a b-barrel. At neutral pH, equine LG (ELG) is monomeric, whereas bovine LG (BLG) is dimeric, and the I-strands of its two subunits form an intermolecular b-sheet. We previously constructed a chimeric ELG in which the sequence of the I-strand was replaced with that of BLG. This chimera did not dimerize. For this study, we constructed the new chimera we call Gyuba (which means cow and horse in Japanese). The amino acid sequence of Gyuba includes the sequences of the BLG secondary structures and those of the ELG loops. The crystal structure of Gyuba is very similar to that of BLG and indicates that Gyuba dimerizes via the intermolecular b-sheet formed by the two I-strands. Thus, the entire arrangement of the secondary structural elements is important for LG dimer formation.

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Structure of bovine β-lactoglobulin (variant A) at very low ionic strength

Cited by 57 publications

References 41 publications

Food protein-stabilized nanoemulsions as potential delivery systems for poorly water-soluble drugs: preparation, in vitro characterization, and pharmacokinetics in rats

Food protein-stabilized nanoemulsions as potential delivery systems for poorly water-soluble drugs: preparation, in vitro characterization, and pharmacokinetics in rats

Structural and dynamic roles of permanent water molecules in ligand molecular recognition by chicken liver bile acid binding protein

Structure and stability of Gyuba, a β‐lactoglobulin chimera

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