Intermolecular disulfide cross-linked structural change induced by permanent wave treatment of human hair with thioglycolic acid

Journal of Cosmetic Science

Volumn 63, Issue 3, 2012, Pages 177-196

  Suzuta, Kazuyuki ^a   Ogawa, Satoshi ^a   Takeda, Yasufumi ^a   Kaneyama, Katsumi ^a   Arai, Kozo ^b  

^a Milbon Co Ltd   (Japan)

^b KRA Wool Research Laboratory   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

2-MERCAPTOACETATE; BROMATE; DISULFIDE; INTERMEDIATE FILAMENT PROTEIN; KERATIN; SODIUM BROMATE; SODIUM DERIVATIVE; THIOGLYCOLIC ACID; THIOGLYCOLIC ACID DERIVATIVE;

ARTICLE; BIOLOGICAL MODEL; CHEMISTRY; DRUG EFFECT; FEMALE; HAIR; HUMAN; MECHANICAL STRESS; METABOLISM; OXIDATION REDUCTION REACTION; ULTRASTRUCTURE;

BROMATES; DISULFIDES; FEMALE; HAIR; HUMANS; INTERMEDIATE FILAMENT PROTEINS; KERATINS; MODELS, BIOLOGICAL; OXIDATION-REDUCTION; SODIUM COMPOUNDS; STRESS, MECHANICAL; THIOGLYCOLATES;

EID: 84872020254     PISSN: 15257886     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (36)

1. H. Bogaty, Molecular forces in permanent waving, J. Soc. Cosmet. Chem., 11, 333–342 (1960).
2. F.-J. Wortmann and N. Kure, Bending relaxation properties of human hair and permanent waving performance, J. Soc. Cosmet. Chem., 41, 123–139 (1990).
3. M. Feughelman, A note on the permanent setting of human hair, J. Soc. Cosmet. Chem., 41, 209–212 (1990).
4. M. Feughelman, A comment on “Bending relaxation properties of human hair and permanent waving performance,” J. Soc. Cosmet. Chem., 42, 129–131 (1991).
5. M. Okano, H. Oka, T. Hatakeyama, and R. Endo, Effect of thiol structures on reduction of hair, J. Soc. Cosmet. Chem. Jpn., 32, 43–51 (1998).
6. A. Kuzuhara and T. Hori, Reduction mechanism of thioglycolic acid on keratin fibers using microspec-trophotometry and FT-Raman spectroscopy, Polymer, 44, 7963–7970 (2003).
7. C. R. Robbins, Chemical and Physical Behavior of Human Hair, 4th Ed. (Springer-Verlag, New York, 2002).
8. S. Ogawa, Y. Takeda, K. Kaneyama, K. Joko, and K. Arai, Chemical reactions occurring in curing treatment for permanent hair straightening using thioglycolic and dithioglycolic acids, Sen’i Gakkaishi, 65, 15–23 (2009).
9. K. Sakurai and K. Joko, Effects of some relaxation treatments on the waving performance of the permanent waving procedure of human hair, Sen’i Gakkaishi, 66, 272–279 (2010).
10. S. Ogawa, K. Fujii, K. Kaneyama, K. Arai, and K. Joko, A curing method for permanent hair straightening using thioglycolic and dithiodiglycolic acids, J. Cosmet. Sci., 51, 379–399 (2000).
11. A. R. Haly and M. Feughelman, Supercontracting and setting behavior of modified wool fibers, Text. Res. J., 30, 365–372 (1960).
12. E. Menefee, physical and chemical consequences of keratin crosslinking, with application to the determination of crosslink density, Adv. Exp. Med. Biol., 86, 307–327 (1977).
13. S. Naito and K. Arai, Type and location of SS linkages in human hair and their relation to fiber properties in water, J. Appl. Polym. Sci., 61, 2113–2118 (1996).
14. K. Arai, G. Ma, and T. Hirata, Crosslinking structure of keratin. III. Rubberlike elasticity originating from non-uniform structures of the swollen hair and wool fibers, J. Appl. Polym. Sci., 42, 1125–1131 (1991).
15. S. Naito, K. Arai, M. Hirano, M. Nagasawa, and M. Sakamoto, Crosslinking structure of keratin. V. Number and type of crosslinks in microstructures of untreated and potassium cyanide treated human hair, J. Appl. Polym. Sci., 61, 1913–1925 (1996).
16. K. Arai, S. Naito, V. B. Dang, N. Nagasawa, and M. Hirano, Crosslinking structure of keratin. VI. Number, type, and location of disulfide crosslinkages in low-sulfur protein of wool fiber and their relation to permanent set, J. Appl. Polym. Sci., 60, 169–179 (1996).
17. K. Arai, N. Sasaki, S. Naito, and T. Takahashi, Crosslinking structure of keratin. I. Determination of the number of crosslinks in hair and wool keratins from mechanical properties of the swollen fiber, J. Appl. Polym. Sci., 38, 1159–1172 (1989).
18. D. Weigmann, L. Rebenfeld, and C. Dansizer, Kinetics and temperature dependence of the chemical stress relaxation of wool fibers, Text. Res. J., 36, 535–542 (1966).
19. K. Arai and T. Hanyu, Rheological properties of swollen wool in concentrated lithium bromide solutions containing mono- or di-ethylene glycol monoalkyl ether, Proc. 6th Int. Wool Text. Res. Conf., Pretoria, 2, 285–294 (1980).
20. M. Feughelman, A two-phase structure for keratin fibers, Text. Res. J., 29, 223–228 (1959).
21. W. G. Crewther, The stress-strain characteristics of animal fibers after reduction and alkylation, Text. Res. J., 35, 867–877 (1965).
22. rd Ed. (Clarendon Press, Oxford, 1975).
23. W. J. Leonard, Jr., Block copolymer elasticity, J. Polym. Sci. Polym. Symp., 54, 237–248 (1976).
24. W. G. Crewther, L. M. Dowling, K. H. Gough, R. C. Marshall, and L. G. Sparrow, “The Microfibrillar Proteins of Alpha-Keratin,” in Fibrous Proteins: Scientific, Industrial and Medical Aspects, D. A. D. Parry and K. Creamer. Eds. (Academic Press, London, 1980), Vol. 2, pp. 151–159.
25. L. Langbein, M. A. Rogers, H. Winter, S. Praetze, and J. Schweizer, The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins, J. Biol. Chem., 276, 35123–35132 (2001).
26. D. A. D. Parry and R. D. B. Fraser, Intermediate filament structure. I. Analysis of IF protein sequence data, Int. J. Biol. Macromol., 7, 203–213 (1985).
27. P. M. Steinert, Structure, function, and dynamics of keratin intermediate filaments, J. Invest. Dermatol., 100, 729–734 (1993).
28. L. C. Gruen and E. F. Woods, Structural studies on the microfibrillar proteins of wool. Interaction between alpha-helical segments and reassembly of a four-chain structure, Biochem. J., 209, 587–595 (1983).
29. J. F. Conway, R. D. B. Fraser, T. P. MacRae, and D. A. D. Parry, “Protein Chains in Wool and Epidermal Keratin IF: Structural Features and Spatial Arrangement,” in The Biology of Wool and Hair, G. E. Rogers, P. J. Reis, K. A. Ward, and R. C. Marshall, Eds. (Chapman and Hall, New York, 1989), pp. 127–144.
30. R. D. B. Fraser, T. P. MacRae, L. G. Sparrow, and D. A. D. Parry, Disulphide bonding in α-keratin, Int. J. Biol. Macromol., 10, 106–112 (1988).
31. J. M. Gillespie, The high-sulfur proteins of α-keratins: Their relation to fiber structure and properties, J. Polym. Sci., Part C, 20, 201–214 (1967).
32. D. S. Fudge, K. H. Gardner, V. T. Forsyth, C. Rickel, and J. M. Gosline, The mechanical properties of hydrated intermediate filaments: Insights from hagfish slime threads, Biophys. J., 85, 2015–2027 (2003).
33. M. Feughelman, Creep of wool fibers in water, J. Text. Inst., 45, T630–T641 (1954).
34. M. Feughelman, Natural protein fibers, J. Appl. Polym. Sci., 83, 489–507 (2002).
35. M. Feughelman and R. Griffith, The relationship between the mechanical properties of α-keratin fibers and the structure of their cortex, Proc. 9th Int. Wool Text. Res. Conf., Biella, 2, 31–43 (1995).
36. F.-J. Wortmann, C. Springob, and G. Sendelbach, Investigations of cosmetically treated human hair by differential scanning calorimetry in water, J. Cosmet. Sci., 53, 219–228 (2002).