684 JOURNAL OF COSMETIC SCIENCE CONCLUSION The work reported herein attempts to demonstrate how experiments performed in the wet state yield only part of the story regarding hair’s physical properties. Specifically, such experiments contain no contribution from the amorphous KAPs, that is, the matrix. Yet, this structure can be the dominant contributor to certain properties, such as fiber stiffness. Furthermore, the results from dry-state experiments, which do include matrix contributions, can produce outcomes contrary to well-established beliefs. For example, damaging chemical treatments can raise hair’s dry-state modulus and produce higher dry- state protein denaturing temperatures. Approaches have been described for modeling the contributions of the various internal structures to hair properties, while similarly incorporating the sizable effects of water content. To this end, experiments at low humidity (i.e., low water content) contain higher contributions from the innate matrix structure, for which the disruptive effects of moisture are minimized. Testing is rarely performed under these conditions, and new insights may be waiting in experiments performed under these conditions. For example, Figure 11 shows results from modulus versus humidity experiments that were performed on different hair samples obtained from a variety of individual donors. These curves superimpose and suggest no differences at high water content, but considerable divergence occurs at low humidity. The properties of hairs obtained from individual heads can be substantially altered by habits and practices yet, all of our donors reported no use of chemical treatments. Moreover, the three behaviors shown in Figure 11 were repeatedly encountered, whereas more random outcomes would presumably be expected if the hairs exhibited substantial contributions from the diversity of consumer practices. In accordance with the principles outlined herein, these mechanical properties imply differences in the internal structures of the hairs from these individuals—particularly in the structure and morphology of the amorphous matrix. This presumption is outside the 0 20 40 60 80 100 1e+9 2e+9 3e+9 4e+9 5e+9 Young’s modulus as a function of RH Relative humidity (%) Behavior 3 Behavior 2 Behavior 1 Figure 11. Differing shapes for Young’s moduli versus RH curves for single-source hairs obtained from different individuals. Yongsmodls
685 THE MATRIX REVISITED limits of conventional thinking with regard to hair structure, but perhaps there are some accepted ideas within the literature that might provide an explanation. Specifically, the existence of different types of cortical cells containing differing quantities of matrix protein has been reported (39). Conceptually, then, a higher proportion of high-sulfur cortical cells would presumably enhance dry-state mechanics while perhaps impacting other related properties, such as diffusion rates into hair fibers. The pursuit of these nonstandard ideas will be the subject of future research activities. REFERENCES (1) M. Feughelman, A two-phase structure for keratin fibers, Text. Res. J., 29(3), 223–228 (1959). (2) D. Persaud and Y. K. Kameth, Torsional method for evaluating hair damage and performance of hair care ingredients, J. Cosmet. Sci., 55(Suppl), S65–S77 (2004). (3) S. Breakspear, B. Noecker, and C. Popescu, Relevance and evaluation of hydrogen and disulfide bond contribution to the mechanics of hard α-keratin fibers, J. Phys. Chem. B, 123(21), 4505−4511 (2019). (4) C. Popescu and H. Höcker, Chapter 4. Cytomechanics of hair. Basics of the mechanical stability, Int. Rev. Cell Mol. Biol., 277(C), 137–156 (2009). (5) J. C. Maxwell, The Bakerian Lecture. On the viscosity or internal friction of air and other gases, Philos. Trans. R. Soc. London, 156, 249–268 (1866). (6) W. Voigt, Kompendium der theoretischen Physik, Band I (De Gruyter, Leipzig, Germany, 1895). (7) A. Tobolsky and H. Eyring, Mechanical properties of polymeric materials. J. Chem. Phys., 11, 125–135 (1943). (8) G. Halsey, H. J. White, Jr., and H. Eyring, Mechanical properties of textiles, I, Text. Res. J., 15(9), 295–311 (1945). (9) C. E. Reese and H. Eyring, Mechanical properties and the structure of hair, Text. Res. J., 20(11), 743–753 (1950). (10) L. Peters and J. B. Speakman, The visco-elastic properties of wool fibers, Text. Res. J., 18(9), 511–518 (1948). (11) M. Feughelman, Natural protein fibers, J. Appl. Polym. Sci., 83(3), 489–507 (2002). (12) F.-J. Wortmann and S. De Jong, Nonlinear viscoelastic behavior of wool fibers in a single step relaxation test. J. Appl. Polym. Sci., 30(5), 2195–2206 (1985). (13) R. D. B. Fraser and D. A. D. Parry, “Trichocyte keratin-associated proteins (KAPs)”, in The Hair Fibre: Proteins, Structure and Development, J. E. Plowman, D. Harland, and S. Deb-Choudhury, Eds. (Springer Nature Singapore Pty Ltd., Singapore, 2018), pp. 71–86. Advances in Experimental Medicine and Biology, vol. 1054. (14) T. W. Mitchell and M. Feughelman, The torsional properties of single wool fibers. Part I: Torque-twist relationships and torsional relaxation in wet and dry fibers. Text. Res. J., 30(9), 662–667, (1960). (15) C. Popescu, Mechanomics, Princeton, New Jersey, September 18–19 2014. 6th International Conference on Applied Hair Science: TRI Princeton. (16) A. H. Nissan, H-bond dissociation in hydrogen bond dominated solids. Macromolecules, 9(5), 840–850 (1976). (17.) Y. Kajiura, S. Watanabe, T. Itou, K. Nakamura, A. Iida, K. Inoue, N. Yagi, Y. Shinohara, and Y. Amemiya, Structural analysis of human hair single fibres by scanning microbeam SAXS. J. Struct. Biol., 155(3), 438–444 (2006). (18) S. Breakspear, The Contribution of Non-Covalent Strategic Bonds to the Nanomechanical Properties of Hair, Redbank, New Jersey, June 8–9 2016, 7th International Conference on Applied Hair Science: TRI Princeton.
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