Hydrophobic in the context of "Contact angle"

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⭐ Core Definition: Hydrophobic

In chemistry, hydrophobicity is the chemical property of a molecule (called a hydrophobe) that is seemingly repelled from a mass of water. In contrast, hydrophiles are attracted to water.

Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents. Because water molecules are polar, hydrophobes do not dissolve well among them. Hydrophobic molecules in water often cluster together, forming micelles. Water on hydrophobic surfaces will exhibit a high contact angle.

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Hydrophobic in the context of Superhydrophobic

In chemistry and materials science, ultrahydrophobic (or superhydrophobic) surfaces are highly hydrophobic, i.e., extremely difficult to wet. The contact angles of a water droplet on an ultrahydrophobic material exceed 150°. This is also referred to as the lotus effect, after the superhydrophobic leaves of the lotus plant. A droplet striking these kinds of surfaces can fully rebound like an elastic ball. Interactions of bouncing drops can be further reduced using special superhydrophobic surfaces that promote symmetry breaking, pancake bouncing or waterbowl bouncing.

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Hydrophobic in the context of Micelle

A micelle (/mˈsɛl/) or micella (/mˈsɛlə/) (pl.micelles or micellae, respectively) is an aggregate (or supramolecular assembly) of surfactant amphipathic lipid molecules dispersed in a liquid, forming a colloidal suspension (also known as associated colloidal system). A typical micelle in water forms an aggregate, with the hydrophilic "head" regions in contact with surrounding solvent, sequestering the hydrophobic single-tail regions in the micelle centre.

This phase is caused by the packing behavior of single-tail lipids in a bilayer. The difficulty in filling the volume of the interior of a bilayer, while accommodating the area per head group forced on the molecule by the hydration of the lipid head group, leads to the formation of the micelle. This type of micelle is known as a normal-phase micelle (or oil-in-water micelle). Inverse micelles have the head groups at the centre with the tails extending out (or water-in-oil micelle).

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Hydrophobic in the context of Transmembrane protein

A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane. Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They frequently undergo significant conformational changes to move a substance through the membrane. They are usually highly hydrophobic and aggregate and precipitate in water. They require detergents or nonpolar solvents for extraction, although some of them (beta-barrels) can be also extracted using denaturing agents.

The peptide sequence that spans the membrane, or the transmembrane segment, is largely hydrophobic and can be visualized using the hydropathy plot. Depending on the number of transmembrane segments, transmembrane proteins can be classified as single-pass membrane proteins, or as multipass membrane proteins. Some other integral membrane proteins are called monotopic, meaning that they are also permanently attached to the membrane, but do not pass through it.

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Hydrophobic in the context of Essential oil

Essential oils are concentrated, hydrophobic liquids containing volatile (readily evaporate) chemical compounds extracted from plant material. Essential oils are also known as volatile oils, ethereal oils, aetheroleum, or simply as the oil of the plant from which they were extracted, such as oil of clove. An essential oil is essential in the sense that the oil contains the fragrance or essence of the plant. The term "essential" used here does not indicate that it is nutritionally required in the diet, as with essential amino acid or essential fatty acid.

Essential oils are most commonly extracted by steam distillation. Other processes include expression, solvent extraction, sfumatura, and cold pressing. They are used in perfumes, cosmetics, soaps, air fresheners and other products, for flavoring food and drink, and for adding scents to household cleaning products.

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Hydrophobic in the context of Cork (material)

Cork is an impermeable buoyant material. It is the phellem layer of bark tissue which is harvested for commercial use primarily from Quercus suber (the cork oak), which is native to southwest Europe and northwest Africa. Cork is composed of suberin, a hydrophobic substance. Because of its impermeable, buoyant, elastic, and fire retardant properties, it is used in a variety of products, the most common of which is wine stoppers.

The montado landscape of Portugal produces approximately half of the cork harvested annually worldwide, with Corticeira Amorim being the leading company in the industry. Cork was examined microscopically by Robert Hooke, which led to his discovery and naming of the cell.

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Hydrophobic in the context of Antistatic

An antistatic agent is a compound used for treatment of materials or their surfaces in order to reduce or eliminate buildup of static electricity. Static charge may be generated by the triboelectric effect or by a non-contact process using a high voltage power source. Static charge may be introduced on a surface as part of an in-mold label printing process.

The role of an antistatic agent is to make the surface or the material itself slightly conductive, either by being conductive itself, or by absorbing moisture from the air; therefore, some humectants can be used. The molecules of an antistatic agent often have both hydrophilic and hydrophobic areas, similar to those of a surfactant; the hydrophobic side interacts with the surface of the material, while the hydrophilic side interacts with the air moisture and binds the water molecules.

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Hydrophobic in the context of Phospholipid

Phospholipids are a class of lipids whose molecule has a hydrophilic "head" containing a phosphate group and two hydrophobic "tails" derived from fatty acids, joined by an alcohol residue (usually a glycerol molecule). Marine phospholipids typically have omega-3 fatty acids EPA and DHA integrated as part of the phospholipid molecule. The phosphate group can be modified with simple organic molecules such as choline, ethanolamine or serine.

Phospholipids are essential components of neuronal membranes and play a critical role in maintaining brain structure and function. They are involved in the formation of the blood-brain barrier and support neurotransmitter activity, including the synthesis of acetylcholine.

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Hydrophobic in the context of Lipid bilayer

The lipid bilayer (or phospholipid bilayer) is a thin polar membrane made of two layers of lipid molecules. These membranes form a continuous barrier around all cells. The cell membranes of almost all organisms and many viruses are made of a lipid bilayer, as are the nuclear membrane surrounding the cell nucleus, and membranes of the membrane-bound organelles in the cell. The lipid bilayer is the barrier that keeps ions, proteins and other molecules where they are needed and prevents them from diffusing into areas where they should not be. Lipid bilayers are ideally suited to this role, even though they are only a few nanometers in width, because they are impermeable to most water-soluble (hydrophilic) molecules. Bilayers are particularly impermeable to ions, which allows cells to regulate salt concentrations and pH by transporting ions across their membranes using proteins called ion pumps.

Biological bilayers are usually composed of amphiphilic phospholipids that have a hydrophilic phosphate head and a hydrophobic tail consisting of two fatty acid chains. Phospholipids with certain head groups can alter the surface chemistry of a bilayer and can, for example, serve as signals as well as "anchors" for other molecules in the membranes of cells. Just like the heads, the tails of lipids can also affect membrane properties, for instance by determining the phase of the bilayer. The bilayer can adopt a solid gel phase state at lower temperatures but undergo phase transition to a fluid state at higher temperatures, and the chemical properties of the lipids' tails influence at which temperature this happens. The packing of lipids within the bilayer also affects its mechanical properties, including its resistance to stretching and bending. Many of these properties have been studied with the use of artificial "model" bilayers produced in a lab. Vesicles made by model bilayers have also been used clinically to deliver drugs.

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Hydrophobic in the context of Protein aggregation

In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease.

After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state. This folding process is driven by the hydrophobic effect: a tendency for hydrophobic (water-fearing) portions of the protein to shield themselves from the hydrophilic (water-loving) environment of the cell by burying into the interior of the protein. Thus, the exterior of a protein is typically hydrophilic, whereas the interior is typically hydrophobic.

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