ArticleBiophysical journal2002
A new deformation model of hard alpha-keratin fibers at the nanometer scale: implications for hard alpha-keratin intermediate filament mechanical properties.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 77 citations in OpenAlex.
- Article
- Synthesis of a new amino acid derivative with long-lasting hair shape control effects and elucidation of its mechanisms.International journal of cosmetic science · 2025Article
- Strain and Strain Recovery of Human Hair from the Nano- to the Macroscale.Life (Basel, Switzerland) · 2023Article
- Protein-Based Biological Materials: Molecular Design and Artificial Production.Chemical reviews · 2023Review
- Porosity at Different Structural Levels in Human and Yak Belly Hair and Its Effect on Hair Dyeing.Molecules (Basel, Switzerland) · 2020Article
- Giant axonal neuropathy alters the structure of keratin intermediate filaments in human hair.Journal of the Royal Society, Interface · 2017Article
- Keratin network modifications lead to the mechanical stiffening of the hair follicle fiber.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Immunolocalization of alpha-keratins and associated beta-proteins in lizard epidermis shows that acidic keratins mix with basic keratin-associated beta-proteins.Protoplasma · 2014Article
- Nanoscale strain-hardening of keratin fibres.PloS one · 2012Article
- Hierarchical structure controls nanomechanical properties of vimentin intermediate filaments.PloS one · 2009Article
- Structure and functions of keratin proteins in simple, stratified, keratinized and cornified epithelia.Journal of anatomy · 2009Review
- A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability.The Journal of cell biology · 2005Article
- New aspects of the alpha-helix to beta-sheet transition in stretched hard alpha-keratin fibers.Biophysical journal · 2004Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanical behavior of human hair fibers is determined by the interactions between keratin proteins structured into microfibrils (hard alpha-keratin intermediate filaments), a protein sulfur-rich matrix (intermediate filaments associated proteins), and water molecules. The structure of the microfibril-matrix assembly has already been fully characterized using electron microscopy and small-angle x-ray scattering on unstressed fibers. However, these results give only a static image of this assembly. To observe and characterize the deformation of the microfibrils and of the matrix, we have carried out time-resolved small-angle x-ray microdiffraction experiments on human hair fibers stretched at 45% relative humidity and in water. Three structural parameters were monitored and quantified: the 6.7-nm meridian arc, which is related to an axial separation between groups of molecules along the microfibrils, the microfibril's radius, and the packing distance between microfibrils. Using a surface lattice model of the microfibril, we have described its deformation as a combination of a sliding process and a molecular stretching process. The radial contraction of the matrix is also emphasized, reinforcing the hydrophilic gel nature hypothesis.
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