THE BINDING OF SMALL MOLECULES TO HAIR--I 469 (18) 09) (20) (21) (22) (23) (24) (25) (26) (27) (28) (29) (30) (31) (32) (33) (34) (35) (36) (37) (38) (39) (40) (41) (42) Malcolm, B. R. Infrared absorption spectrum of water adsorbed on a-helical synthetic polypeptides. Nature (London) 227 1358 (1970). Baddiel, C. B., Breuer, M. M. and Stephens, R. J. J. ColloidInterface Sci. (in press). Puffr, R. and Sebenda, J. The structure and properties of polyamides XXVII. The mecha- nism water sorption in polyamides. J. Polymer Sci. Part C. 16 79 (1966). Tsuboi, M. Molecular state of water bound to the peptide linkage. Bull. Chem. Soc. Japan 25 160 (1952). Ilkegami, A. Hydration of polyacids. Biopolymers 6 431 (1968). Strauss, U. P. and Leung, Y. P. Volume changes as a criterion for site binding of counterions by Polyelectrolytes. J. Amer. Chem. Soc. 87 1476 (1965). Breuer, M. M. Volume changes accompanying binding of phenols by hair. J. Phys. Chem. 68 2081 (1964). Clifford, J. and Pethica, B. A. Properties of micellar solutions. Pt 2. N.m.r. chemical shift of water protons in solutions of sodium alkyl sulphates. Trans. Faraday Soc. 60 1483 (1964). Corkill, J. M., Goodman, J. F. and Tate, J. R. Heats of solution of alkylhexaoxyethylene glycol monoethers. Trans. Faraday Soc. 63 773 (1967). Clifford, J., Oakes, J. and Tiddy, G. J. T. Special discussions of the Faraday Society on thin liquid films and boundary layers 175 (1) (1970) (Academic Press, London). Timasheff, S. N. and Pittz, E. P. American Chemical Society, 161st National Meeting Pro- ceedings, Paper Coll. 9 (1971) (American Chemical Society, Washington). Feughelman, M. The mechanical properties of set wool fibres and the structure of keratin. J. Text. Inst. 51 T589 (1960). Skertchly, A. and Woods, H. J. The a .•- It transformation in keratin. J. Text. Inst. 51 T517 (1960). Flory, P. J. Theory of elastic mechanisms in fibrous proteins. J. Amer. Chem. Soc. 78 5222 (1956). Ciferri, A. The a 13 transformation in keratin. Trans. Faraday Soc. 56 562 (1963). Mandelkern, L., Halpin, J. C., Diorio, A. F. and Posner, A. S. Dimensional changes in fibrous macromolecules. The system a-keratin-lithium bromide. J. Amer. Chem. Soc. 84 1383 (1962). Mandelkern, L. Crystallisation ofpolymers (1964) (McGraw-Hill, New York). Breuer, M. M. Acid titration of keratin and its implication regarding keratin structure. Trans. Faraday $oe. 60 1003 (1964). David, C. W., Haukaas, H. B., Kalnins, J. G. and Schor, R. Statistical-mechanical studies of the a 13 transformation in keratins. The tension-length isotherms. Biophys. J. 7 505 (1967). Breuer, M. M. Strain-stress isotherm of keratin fibers. Biopolymers 6 1503 (1968). Haly, A. R. Stress-strain behavior and volume swelling of wool fibers rendered elastomeric in a LiBr solution. Kolloid-Z 191 105 (1963). Breuer, M. M. Proceedings 1st European Biophysics Conference, Baden, Wien, September 1971.5 449 (1971) (Verlag der Wiener Medizinischen Akademie, Vienna). Haly, A. R. and Snaith, J. W. Differential thermal analysis of wool The phase-transition endotherm under various conditions. Text. Res. J. 37 899 (1967). Bull, H. B. Adsorption of water vapor by proteins. J. Amer. Chem. Soc. 66 1499 (1944). Ebert, G., Ebert, Ch. and Wendorff, J. Fibrous keratins. Chemical and physical investiga- tions of fibrous keratins influence of internal and external parameters on supercontraction. Kolloid-Z. Z. Polymer 237 229 (1970).
J. Soc. Cosmet. Chem. 23 471479 (1972) ¸ 1972 Society of Cosmetic Chemists of Great Britain The effect of saturated salt solutions on the elastic properties of stratum corneum A. C. PARK and C. B. BADDIEL* Synopsis--ELASTIC MODULUS values have been obtained for native and solvent extracted STRATUM CORNEUM in saturated SOLUTIONS of various SALTS. In nearly every case the modulus was lowered significantly relative to its value at the same equivalent water activity in the vapour phase. This effect was attributed to disruption of the protein matrix of the CELL junctions which are believed to be responsible for the mechanical integrity of the corneum. A simple structural model is proposed which accounts for the response of the corneum to various TREATMENTS. INTRODUCTION The protection of the body against environmental hazards is main- tained by a thin layer of dead cells called the stratum corneum. The function of this outermost layer of the skin is to act as a barrier between the environ- ment and the complex system of living tissues which it covers. In the in vivo situation the stratum corneum must be able to respond quickly and without damage to mechanical stresses and strains imposed on it by various perturbations. As a result, studies in this and other laboratories (1-6) have been based on the premises that (i) maintenance of the mechanical integrity of this layer is important if it is to continue to fulfil its proper protective role, and (ii) changes in its mechanical properties can be used as a probe of those factors which influence its function and structure. The principal constituent (60-70•o dry weight), of the stratum corneum is a soft form of the fibrous protein, keratin, which is contained within the * Unilever Research Laboratory, 455 London Road, Isleworth, Middlesex. 471
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