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1.
Proc Natl Acad Sci U S A ; 113(21): 5940-5, 2016 May 24.
Article in English | MEDLINE | ID: mdl-27162354

ABSTRACT

The complex mechanical properties of biomaterials such as hair, horn, skin, or bone are determined by the architecture of the underlying fibrous bionetworks. Although much is known about the influence of the cytoskeleton on the mechanics of isolated cells, this has been less studied in tridimensional tissues. We used the hair follicle as a model to link changes in the keratin network composition and architecture to the mechanical properties of the nascent hair. We show using atomic force microscopy that the soft keratinocyte matrix at the base of the follicle stiffens by a factor of ∼360, from 30 kPa to 11 MPa along the first millimeter of the follicle. The early mechanical stiffening is concomitant to an increase in diameter of the keratin macrofibrils, their continuous compaction, and increasingly parallel orientation. The related stiffening of the material follows a power law, typical of the mechanics of nonthermal bending-dominated fiber networks. In addition, we used X-ray diffraction to monitor changes in the (supra)molecular organization within the keratin fibers. At later keratinization stages, the inner mechanical properties of the macrofibrils dominate the stiffening due to the progressive setting up of the cystine network. Our findings corroborate existing models on the sequence of biological and structural events during hair keratinization.


Subject(s)
Hair Follicle/chemistry , Hair Follicle/metabolism , Keratins/chemistry , Keratins/metabolism , Humans
2.
Appl Spectrosc ; 68(5): 564-9, 2014.
Article in English | MEDLINE | ID: mdl-25014600

ABSTRACT

Atomic force microscopy (AFM) and infrared (IR) spectroscopy have been combined in a single instrument (AFM-IR) capable of producing IR spectra and absorption images at a sub-micrometer spatial resolution. This new device enables human hair to be spectroscopically characterized at levels not previously possible. In particular, it was possible to determine the location of structural lipids in the cuticle and cortex of hair. Samples of human hair were embedded, cross-sectioned, and mounted on ZnSe prisms. A tunable IR laser generating pulses of the order of 10 ns was used to excite sample films. Short duration thermomechanical waves, due to infrared absorption and resulting thermal expansion, were studied by monitoring the resulting excitation of the contact resonance modes of the AFM cantilever. Differences are observed in the IR absorbance intensity of long-chain methylene-containing functional groups between the outer cuticle, middle cortex, and inner medulla of the hair. An accumulation of structural lipids is clearly observed at the individual cuticle layer boundaries. This method should prove useful in the future for understanding the penetration mechanism of substances into hair as well as elucidating the chemical nature of alteration or possible damage according to depth and hair morphology.


Subject(s)
Hair/chemistry , Hair/ultrastructure , Lipids/analysis , Microscopy, Atomic Force/methods , Nanotechnology/methods , Spectrophotometry, Infrared/methods , Equipment Design , Hair Preparations/chemistry , Hair Preparations/pharmacokinetics , Humans , Keratins/chemistry , Keratins/ultrastructure , Lasers , Microscopy, Atomic Force/instrumentation , Nanotechnology/instrumentation , Specimen Handling , Spectrophotometry, Infrared/instrumentation , Spectroscopy, Fourier Transform Infrared/methods , Vibration
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