Keratin water binding

The authors speculated that this phenomenon might have been due to increased salt content of the skin caused by the rofecoxib, resulting in increased water-binding capacity of keratin. 

Unraveling the molecular mechanism of water binding by keratins (e.g., wool, hair, nails, etc.) has interested chemists for half a century ()L). Essentially, two types of models have been suggested for explaining water absorption isotherms of keratins one that postulates the binding of water mol-... 

Therefore, we feel that we are now in a posi-tTon to carry out a rigorous thermodynamic analysis of the water-keratin interaction process, and to examine critically the various water binding theories by comparing the experimentally determined thermodynamic changes at constant volume with those predicted by the various theories. 

Since statistical mechanical models for water binding are generally derived for constant volume condition, a comparison of experimental data with the calculated models is only possible provided the value of AGg can be calculated or estimated. So far, this has not been the case for the water-keratin interaction. 

The structural and functional properties of the cutaneous surface almost entirely are those of the stratum comeum, modified only slightly by influences of hair, sweat glands and sebaceous glands. The process of keratinization, consisting of the aggregate events by which the epidermis forms the stratum comeum, must be reviewed not only in context with epidermal syntheses of fibrous proteins, mucopolysaccharides and special compounds that modify the texture of the stratum comeum but with other epidermal attributes such as rates of stratum comeum production, and cohesiveness of stratum comeum cells, their hydrophilic and water-binding properties, their elasticity and pliability. 

Bonding Forces Between Dye and Fiber. Dye anions can participate in ionic interactions with fibers that possess cationic groups. However, the formation of ionic bonds is not sufficient to explain dye binding, because compounds that can dissociate are cleaved in the presence of water. Secondary bonds (dispersion, polar bonds, and hydrogen bonds) are additionally formed between dye and fiber [47], Close proximity between the two is a prerequisite for bond formation. However, this is counteracted by the hydration spheres of the dye and of wool keratin. On approach, these spheres are disturbed, especially at higher temperature, and common hydration spheres are formed. The entropy of the water molecules involved is increased in this process (hydrophobic bonding). In addition, coordinate and covalent bonds can be superimposed on secondary and ionic bonds. 

A weakening of the binding forces between the keratinized epithelium and the layer of grease via the reduction of the surface tension between the water and the water-resistant oil/grease. Because of this reduced surface tension, water (and surfactant molecules) can penetrate into the finest wrinkles of the skin. In this way, more and more interface is occupied by surfactant, and the adhesiveness of the soil-containing layer is further weakened, a process facilitated by mechanical rubbing. 

Scleroproteins. Insoluble in water and neutral solvents and resistant to enzymic hydrolysis. These are fibrous proteins serving structural and binding purposes. Collagen of muscle tissue is included in this group, as is gelatin, which is derived from it. Other examples include elastin, a component of tendons, and keratin, a component of hair and hoofs. 

A protein called keratin is insoluble in water but binds to other keratin molecules to form hard structures. Proteins like keratin are... 

A protein called keratin is insoluble in water but binds to other keratin molecules to form hard structures. Proteins like keratin are known as structural proteins or fibrous proteins. Keratin is the main component in hair and fingernails. A different protein called insulin is soluble in water and achieves a certain shape as an individual molecule. Proteins like insulin are known as globular proteins. Insulin in the bloodstream regulates glucose metabolism. 

Dye staining tests [29, 30] show that substantivity of monofunctional cationics to water rinsing does not occur unless the hydrocarbon portion is approximately 8 to 10 carbon atoms. This effect occurs because, in addition to the electrostatic bond, sufficient Van der Waals attractive forces must exist to bind the molecule to the keratin in the presence of the aqueous phase. As the molecular size of the cationic structure is increased, even... 

The way in which water softens the stratum corneum appears to be performed at a rather macroscopic level, i.e. by its filling inter- and intracellular spaces of the dead corneocj es, and to some extent perhaps at the molecular level by binding to cell protein macromolecules, both keratinous and non-keratinous. The aggregate result, however, is to provide an aqueous lubricating system for the cellular lattice structure of the stratum corneum, a lubrication that accounts for unusual pliability of the stratum corneum. 

Low molecular weight pectin can be easily manipulated to design novel materials to eliminate the allergic response by the enzyme. It can bind to enzymes and can cause immimogenic responses. In a similar way, it binds to keratin, forming a hybrid with more water resistance. 

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