Deep sea osmolytes in action: their effect on protein–ligand binding under high pressure stress

Kamali, Armin; Jahmidi-Azizi, Nisrine; Oliva, Rosario; Winter, Roland

doi:10.1039/d2cp01769e

Cited by 13 publications

(17 citation statements)

References 65 publications

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“…The CD spectrum of BSA in neat buffer (Figure 4A) is characterized by two minima, located at ∼222 and ∼209 nm, and a positive band raising at 200 nm. These features are indicative of a protein adopting mainly an α‐helical structure, in agreement with previously reported data and the crystal structure of BSA [12,18] . Upon addition of EA, the general shape of the spectrum was unaffected.…”

Section: Resultssupporting

confidence: 91%

“…The high‐pressure binding data revealed that the binding volume (Table 1) for the interaction of EA with BSA is positive, indicating that the complex occupies a larger volume with respect to the uncomplexed state. A Δ V b °>0 can be ascribed to an increase of void volume in the binding pocket upon complex formation and/or the release of hydration water to the bulk solvent [15,18,25] . Instead, for IB7‐14, the binding volume is essentially zero, revealing an almost perfect packing between the interacting partners.…”

Section: Discussionmentioning

confidence: 99%

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Alcohol‐Induced Conformation Changes and Thermodynamic Signatures in the Binding of Polyphenols to Proline‐Rich Salivary Proteins

Jahmidi‐Azizi,

Oliva,

Winter

2023

Chemistry A European J

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The first contact of polyphenols (tannins) with the human body occurs in the mouth, where they are known to interact with proline‐rich proteins (PRPs). These interactions are important at a sensory level, especially for the development of astringency, but affect also various other biochemical processes. Employing thermodynamic measurements, fluorescence and CD spectroscopy, we investigated the binding process of the prototypical polyphenol ellagic acid (EA) to different IB‐PRPs and BSA, also in the presence of ethanol, which is known to influence tannin–protein interactions. Binding of EA to BSA and the small peptide IB7‐14 is weak, but very strong to IB9‐37. The differences in binding strength and stoichiometry are due to differences in the binding motifs, which also lead to differences in the thermodynamic signatures of the binding process. EA binding to BSA is enthalpy‐driven, whereas binding to both IB7‐14 and IB9‐37 is entropy‐driven. The presence of 10 vol.% EtOH, as present in wines, increases the binding constant of EA with BSA and IB7‐14 drastically, but not that with IB9‐37; however, it changes the binding stoichiometry. These differences can be attributed to the effect of EtOH on the conformation dynamics of the proteins and to changes in hydration properties in alcoholic solution.

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Section: Resultssupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Alcohol‐Induced Conformation Changes and Thermodynamic Signatures in the Binding of Polyphenols to Proline‐Rich Salivary Proteins

Jahmidi‐Azizi,

Oliva,

Winter

2023

Chemistry A European J

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“…The CD spectrum of HSA showed two negative bands at 208 and 220 nm, and a positive band around 195 nm, indicative of the presence of an α-helix structure [ 77 ], in agreement with previously reported CD data and the deposited protein crystal structure [ 76 , 78 ]. Conversely, the CD spectrum of hTf showed a distinct minimum around 210 nm, a weak negative band around 220 nm, and a positive band at 195 nm.…”

Section: Resultssupporting

confidence: 90%

Investigating the Interaction of an Anticancer Nucleolipidic Ru(III) Complex with Human Serum Proteins: A Spectroscopic Study

Riccardi¹,

Campanella²,

Montesarchio

et al. 2023

Molecules

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Ruthenium(III) complexes are very promising candidates as metal-based anticancer drugs, and several studies have supported the likely role of human serum proteins in the transport and selective delivery of Ru(III)-based compounds to tumor cells. Herein, the anticancer nanosystem composed of an amphiphilic nucleolipid incorporating a Ru(III) complex, which we named DoHuRu, embedded into the biocompatible cationic lipid DOTAP, was investigated as to its interaction with two human serum proteins thought to be involved in the mechanism of action of Ru(III)-based anticancer drugs, i.e., human serum albumin (HSA) and human transferrin (hTf). This nanosystem was studied in comparison with the simple Ru(III) complex named AziRu, a low molecular weight metal complex previously designed as an analogue of NAMI-A, decorated with the same ruthenium ligands as DoHuRu but devoid of the nucleolipid scaffold and not inserted in liposomal formulations. For this study, different spectroscopic techniques, i.e., Fluorescence Spectroscopy and Circular Dichroism (CD), were exploited, showing that DoHuRu/DOTAP liposomes can interact with both serum proteins without affecting their secondary structures.

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“…Kamali copy, supplemented by CD spectroscopy, and computer modeling. 76 They showed that, depending on the local chemical composition of the protein's binding pocket, there are osmolytes with specific interaction sites and hydration free energies capable of mediating efficient ligand binding even under pressure stress conditions. In the binding of proflavine to BSA and HSA, the addition of both cosolvents resulted in an increase in the binding constant at high pressure, with TMAO being the most efficient one.…”

Section: Volume-sensitive Conformational Changes Phase Transitions An...mentioning

confidence: 99%

“…The accompanying decrease of the configurational entropy of the protein and ligand upon binding leads to an overall enthalpy-driven binding process. Kamali et al studied the binding of the ligand proflavine to two serum proteins having different binding pockets (BSA and HSA) in the presence of two deep-sea osmolytes, TMAO and glycine betaine, employing pressure-dependent fluorescence spectroscopy, supplemented by CD spectroscopy, and computer modeling . They showed that, depending on the local chemical composition of the protein’s binding pocket, there are osmolytes with specific interaction sites and hydration free energies capable of mediating efficient ligand binding even under pressure stress conditions.…”

mentioning

confidence: 99%

Harnessing Pressure-Axis Experiments to Explore Volume Fluctuations, Conformational Substates, and Solvation of Biomolecular Systems

Oliva

Winter

2022

J. Phys. Chem. Lett.

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Intrinsic thermodynamic fluctuations within biomolecules are crucial for their function, and flexibility is one of the strategies that evolution has developed to adapt to extreme environments. In this regard, pressure perturbation is an important tool for mechanistically exploring the causes and effects of volume fluctuations in biomolecules and biomolecular assemblies, their role in biomolecular interactions and reactions, and how they are affected by the solvent properties. High hydrostatic pressure is also a key parameter in the context of deep-sea and subsurface biology and the study of the origin and physical limits of life. We discuss the role of pressure-axis experiments in revealing intrinsic structural fluctuations as well as high-energy conformational substates of proteins and other biomolecular systems that are important for their function and provide some illustrative examples. We show that the structural and dynamic information obtained from such pressure-axis studies improves our understanding of biomolecular function, disease, biological evolution, and adaptation.

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Deep sea osmolytes in action: their effect on protein–ligand binding under high pressure stress

Abstract: Because organisms living in the deep sea and in the subseafloor must be able to cope with hydrostatic pressures up to 1000 bar and more, their biomolecular processes, including ligand-binding...

Cited by 13 publications

References 65 publications

Alcohol‐Induced Conformation Changes and Thermodynamic Signatures in the Binding of Polyphenols to Proline‐Rich Salivary Proteins

Alcohol‐Induced Conformation Changes and Thermodynamic Signatures in the Binding of Polyphenols to Proline‐Rich Salivary Proteins

Investigating the Interaction of an Anticancer Nucleolipidic Ru(III) Complex with Human Serum Proteins: A Spectroscopic Study

Harnessing Pressure-Axis Experiments to Explore Volume Fluctuations, Conformational Substates, and Solvation of Biomolecular Systems

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