Physics Maths Engineering
Qiang Sun
Peer Reviewed
Hydrophobic interactions are involved in and believed to be the fundamental driving force of many chemical and biological phenomena in aqueous environments. This review focuses on our current understanding on hydrophobic effects. As a solute is embedded into water, the interface appears between solute and water, which mainly affects the structure of interfacial water (the topmost water layer at the solute/water interface). From our recent structural studies on water and air-water interface, hydration free energy is derived and utilized to investigate the origin of hydrophobic interactions. It is found that hydration free energy depends on the size of solute. With increasing the solute size, it is reasonably divided into initial and hydrophobic solvation processes, and various dissolved behaviors of the solutes are expected in different solvation processes, such as dispersed and accumulated distributions in solutions. Regarding the origin of hydrophobic effects, it is ascribed to the structural competition between the hydrogen bondings of interfacial and bulk water. This can be applied to understand the characteristics of hydrophobic interactions, such as the dependence of hydrophobic interactions on solute size (or concentrations), the directional natures of hydrophobic interactions, and temperature effects on hydrophobic interactions.
Hydrophobic interactions are forces that occur when nonpolar solutes are immersed in water. They are considered fundamental driving forces in many chemical and biological processes that take place in aqueous environments. These interactions play a critical role in processes such as protein folding, molecular aggregation, and the behavior of lipids in biological membranes.
The interface between a solute and water is crucial in determining the structure of interfacial water, which refers to the topmost water layer at the solute/water interface. The presence of the solute disrupts the normal hydrogen bonding network of water, leading to changes in the structure of the interfacial water. These structural changes are key to understanding the origin of hydrophobic interactions.
Hydration free energy is an important quantity in understanding hydrophobic interactions. It is derived from studies of water and the air-water interface. Hydration free energy depends on the size of the solute; as the solute size increases, the hydration free energy also changes. The hydration process can be divided into initial and hydrophobic solvation processes, influencing how solutes behave in solution, such as whether they disperse or accumulate.
The hydrophobic effect is influenced by solute size. As the solute size increases, hydration free energy undergoes changes, which in turn affects the behavior of solutes in solution. Larger solutes experience different solvation processes compared to smaller ones, which can result in varied distributions, either dispersed or accumulated, in the aqueous medium.
The origin of hydrophobic interactions is attributed to the structural competition between the hydrogen bonds of interfacial water and bulk water. When a nonpolar solute is introduced into water, the ordering of water molecules at the interface disrupts the hydrogen bond network in bulk water. This leads to the formation of ordered structures at the solute-water interface, which drives the solute to minimize contact with water, a phenomenon referred to as the hydrophobic effect.
Temperature and concentration influence hydrophobic interactions by affecting the structure and dynamics of the water molecules involved in the interaction. At different temperatures, the behavior of water and solutes can change, altering the strength and nature of hydrophobic interactions. Similarly, solute concentration can impact the degree of hydrophobic effects by changing the extent of solute-solvent interaction and the competition between interfacial and bulk water.
Some key characteristics of hydrophobic interactions include:
This review enhances our understanding of hydrophobic effects by presenting the current insights into the structure of interfacial water and the role of hydration free energy in hydrophobic interactions. It provides a deeper understanding of how solute size, temperature, and solute-water interface dynamics contribute to the behavior of hydrophobic interactions, offering new perspectives on how these effects can be applied to various scientific fields, such as chemistry and biology.
The competition between the hydrogen bonds in interfacial and bulk water is fundamental to the hydrophobic effect. The ordering of water molecules at the solute-water interface disturbs the hydrogen bond network in the bulk water, creating a free energy cost. This structural competition is a key factor driving the tendency for nonpolar solutes to avoid interacting with water, leading to the characteristic behavior observed in hydrophobic interactions.
Understanding hydrophobic interactions has significant implications for fields such as drug design, protein folding, molecular aggregation, and materials science. By understanding how solutes behave in aqueous environments, scientists can design better drugs, create new materials with desired properties, and gain insight into biological processes such as the formation of cell membranes and protein-ligand binding.
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Show by month | Manuscript | Video Summary |
---|---|---|
2025 April | 1 | 1 |
2025 March | 63 | 63 |
2025 February | 44 | 44 |
2025 January | 47 | 47 |
2024 December | 53 | 53 |
2024 November | 59 | 59 |
2024 October | 20 | 20 |
Total | 287 | 287 |