Structural and thermodynamic studies of binding saturated fatty acids to bovine β-lactoglobulin

Loch, J.I.; Polit, Agnieszka; Bonarek, Piotr; Olszewska, D.; Kurpiewska, Katarzyna; Dziedzicka-Wasylewska, Marta; Lewiński, K.

doi:10.1016/j.ijbiomac.2012.03.002

Cited by 86 publications

(114 citation statements)

References 57 publications

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“…In five of the six best models, the hydrophobic chain reached the bottom of the binding pocket in a position similar to that observed for 16-and 18-carbon fatty acids (Fig. 5A) [27]. Differences between models concerned mostly conformation and the position of the morpholine ring; however, all models indicated the possibility of pramocaine binding in the ␤-barrel.…”

Section: Docking Studies Vs Crystal Structuressupporting

confidence: 67%

“…S1). Calculations were performed according to formulas described previously [27]. The protein concentration was corrected based on the activity determined from SDS binding experiments conducted under the same conditions and according to previous studies [28].…”

Section: Isothermal Titration Calorimetrymentioning

confidence: 99%

“…However, the association constant range of 10 2 -10 4 M −1 indicates very weak interactions in comparison to endogenous ligands like fatty acids (10 5 -10 9 M −1 ) [27,44].…”

Section: Calorimetric Studies On Binding Tet and Prm To Blg And Glgmentioning

confidence: 99%

“…As we succeeded to crystallise the GLG-PRM complex only using ammonium sulphate as a precipitant, to check if the crystallisation conditions affect protein-ligand interactions, we also decided to crystallise the BLG-PRM complex in similar conditions. Despite the different crystallisation conditions, all crystals of bovine ␤-lactoglobulin complexes with pramocaine and tetracaine, as well as caprine lactoglobulin complex with PRM, have the symmetry of the P3 2 21 space group typical for other known BLG-ligand complexes available in PDB [7,27,28,52,53]. In all structures, the entrance to the binding pocket is located close to the crystallographic twofold axis, and the relatively short distance between symmetry related molecules might affect geometry at the entrance to the binding site.…”

Section: Crystal Structures Of Lactoglobulin Complexes With Pramocainmentioning

confidence: 99%

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β-Lactoglobulin interactions with local anaesthetic drugs – Crystallographic and calorimetric studies

Loch

Bonarek

Polit

et al. 2015

International Journal of Biological Macromolecules

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Section: Docking Studies Vs Crystal Structuressupporting

confidence: 67%

Section: Isothermal Titration Calorimetrymentioning

confidence: 99%

“…However, the association constant range of 10 2 -10 4 M −1 indicates very weak interactions in comparison to endogenous ligands like fatty acids (10 5 -10 9 M −1 ) [27,44].…”

Section: Calorimetric Studies On Binding Tet and Prm To Blg And Glgmentioning

confidence: 99%

Section: Crystal Structures Of Lactoglobulin Complexes With Pramocainmentioning

confidence: 99%

See 2 more Smart Citations

β-Lactoglobulin interactions with local anaesthetic drugs – Crystallographic and calorimetric studies

Loch

Bonarek

Polit

et al. 2015

International Journal of Biological Macromolecules

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“…The initial crystal structure analyses have shown that most ligands are bound to the internal cavity of the β-barrel [31][32][33]. Besides the primary drug binding site in the internal cavity of the β-barrel, some compounds, such as p-nitrophenyl phosphate, 5-fluorocytosine, ellipticine and protoporphyrin, bind to the outer surface site [34,35].…”

Section: Molecular Docking Studiesmentioning

confidence: 99%

In Silico Study on the Interaction of Thiazolidinediones and β-Lactoglobulin by Molecular Dynamics and Docking Approach

Khosravi

Heidari-Koholi

2015

Journal of Macromolecular Science, Part B

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Thiazolidinediones are widely used in the treatment of diabetes mellitus type 2. An investigation of their interaction with a transport protein, such as β-lactoglobulin (BLG), at the atomic level could be a valuable factor in controlling their transport to biological sites. The interaction of troglitazone, pioglitazone and rosiglitazone, as representative thiazolidinediones, and BLG, as a transport protein, was investigated using molecular docking and molecular dynamics (MD) simulation methods. The molecular docking results showed that these thiazolidinediones bind to the internal cavity of BLG and the BLG affinity for binding the thiazolidinediones decreases in the following order: troglitazone > pioglitazone > rosiglitazone. The analysis of MD simulation trajectories showed that the BLG and BLG-thiazolidinedione complexes became stable at approximately 2500 ps and that there was little conformational change in the BLGDownloaded by [New York University] at 00:42 05 August 2015 ACCEPTED MANUSCRIPT ACCEPTED MANUSCRIPT 2 thiazolidinedione complexes over a 10 ns timescale. In addition, the profiles of atomic fluctuations showed the rigidity of the ligand-binding site during the simulation time.

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Ligand entry into the calyx of β‐lactoglobulin

Bello

García‐Hernández

2014

Biopolymers

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Although the thermodynamic principles that control the binding of drug molecules to their protein targets are well understood, the detailed process of how a ligand reaches a protein binding site has been an intriguing question over decades. The short time interval between the encounter between a ligand and its receptor to the formation of the stable complex has prevented experimental observations. Bovine β-lactoglobulin (βlg) is a lipocalin member that carries fatty acids (FAs) and other lipids in the cellular environment. Βlg accommodates a FA molecule in its highly hydrophobic cavity and exhibits the capability of recognizing a wide variety of hydrophobic ligands. To elucidate the ligand entry process on βlg, we report molecular dynamics simulations of the encounter between palmitate (PA) or laurate (LA) and βlg. Our results show that residues localized in loops at the cavity entrance play an important role in the ligand penetration process. Analysis of the short-term interaction energies show that the forces operating on the systems lead to average conformations very close to the crystallographic holo-forms. Whereas the binding free energy analysis using the molecular mechanics Generalized Born surface area method shows that these conformations were thermodynamically favorable.

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Structural and thermodynamic studies of binding saturated fatty acids to bovine β-lactoglobulin

Cited by 86 publications

References 57 publications

β-Lactoglobulin interactions with local anaesthetic drugs – Crystallographic and calorimetric studies

β-Lactoglobulin interactions with local anaesthetic drugs – Crystallographic and calorimetric studies

In Silico Study on the Interaction of Thiazolidinediones and β-Lactoglobulin by Molecular Dynamics and Docking Approach

Ligand entry into the calyx of β‐lactoglobulin

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