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Nanomechanics of single keratin fibres: A Raman study of the α‐helix →β‐sheet transition and the effect of water

2006/12/03 by Raphaël Paquin, Philippe Colomban
Biochemistry, Genetics and Molecular Biology · Engineering · Materials Science · #Dyeing and Modifying Textile Fibers #Silk-based biomaterials and applications #Skin and Cellular Biology Research

paper · pdf · doi:10.1002/jrs.1672

openalex publication_date 2006/12/03 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/28

Abstract

Abstract The use of micro‐Raman spectroscopy, through chemical‐bond, nano‐scale probes, allows the changes in conformations (α‐helix →β‐sheet), chain orientation, breakage of disulfide bonds (20%) and the increase of intra‐ and inter‐chain distances during the application of stress to be distinguished. The combination of micro‐Raman spectroscopy and a Universal Fibre Tester allows a quantitative measurement of the extension of chemical bonds in the peptide chain during loading. The nano‐structural transformations of keratin during strain of human hair in a dry environment (40–60% relative humidity) and saturated with water have been studied. Water permits the sliding of the chains and decreases the bond energy of the hair. Spectral analyses and 2D correlation are two coherent and independent methods to follow the structural nano‐mechanical (Raman) and micro‐mechanical (strain/stress) analyses, and confirm the validity of the experimental results, tools and principles used, as well as the agreement with the structural model of keratin fibres described by Chapman and Hearle. Copyright © 2006 John Wiley & Sons, Ltd.

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