Keratin made micro-tubes: The paradoxical thermal behavior of cortex and cuticle.

Keratin micro-tubes were obtained by heating medullated keratin fibres to temperatures above 230°C under nitrogen atmosphere, when, as documented by microscopy, the cortex (the core of the fibre) melts from the medulla outwards, followed by pyrolysis of the material through the remaining solid cuticle (shell) layer. The resulted hollow tubes from fibres void of cortical material keep the external cuticle structure, as shown by AFM investigation, and the moisture sorption properties of the initial keratin fibre. Despite similar amino-acid compositions of cuticle and cortex the two morphological components differ significantly in their thermal behaviour, which appears to be a "cortex-cuticle thermal stability paradox".

Prevention of hair surface aging.

The hydrophobic character of the surface of human hair is particularly attributed to the lipid components of the epicuticle and to a layer of covalently bound fatty acids. This outer f-layer mainly consists of 18-methyl eicosanoic acid (18-MEA), which is covalently bound to the underlying protein matrix, forming the epicuticle as composite surface structure. Daily weathering and chemical treatments, specifically oxidative bleaching, decrease the hydrophobicity of the outer hair surface drastically.Multiple daily stress, simulated by an automatic test device including shampooing, blow drying and sun light exposure, changed the lipid composition of hair significantly. A marked loss of 18-MEA was observed. Decreasing contact angles are the direct consequence. A new method to determine the "pseudo-static" contact angle on hair was developed. The results correlate with the corresponding data obtained by dynamic contact angle measurements according to Wilhelmy. Besides that, the resorption time of water droplets by the hair surface provides additional information about the intactness of the outer f-layer.Specific proteolipids, which are lipid-modified keratins, are able to reconstruct the surface layer of damaged hair by creating renewed surface hydrophobicity and extending the water resorption time by the hair surface.

Structural stability of wild type and mutated alpha-keratin fragments: molecular dynamics and free energy calculations.

The objective of this study is to investigate the influence of point mutations on the structural stability of coiled coil fragments of the human hair intermediate filament by molecular dynamics simulations and free energy calculations. Mutations in the helix termination motif of human hair keratin gene hHb6 seem to be connected to the hereditary hair dystrophy Monilethrix. The most common mutations reported are Glu413Lys and Glu413Asp, located at the C-terminal end of the coiled coil 2B rod domain of the IF. According to our simulations, significant conformational changes of the side chains at the mutation and neighboring sites occur due to the Glu413Lys mutation. Furthermore, the differences in electrostatic interactions cause a large change in free energy during transformation of Glu413 to Lys calculated by the thermodynamic integration approach. It is speculated that the structural rearrangement necessary to adapt the interactions in the mutated coiled coil leads to changes in the IF assembly or its stability. The second mutation, Glu413Asp, only leads to a small value of the calculated free energy difference that is within the error limits of the simulations. Thus, it has to be concluded that this mutation does not affect the coiled coil stability.

The structural influence in the stability of polymer-bound diazonium salts.

Various new diazonium ions on a polymeric support that have a variety of counterions and complexation with crown ethers have been prepared, and the thermal stability of these resins over a larger temperature interval has been investigated. Nonisothermal kinetics applied to DSC data have been used predicting the lifetime of the resins.