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9, 1970)
INTRODUCTION
Preliminary 0 bservations
Stabilizedaqueoussolutionsof H202 undergolittle decomposition
at ambient temperatureseven at high pH values. However, the in-
troduction of a solid into a system brings about an increase in the
decompositionrate which is roughly proportional to the surfacearea
of the solid. An additional incrementin the rate of decompositionis
observedwhenever the introduced solid undergoeschemical reaction
with H202. Table I shows the rate differences obtained under such
conditions.
Table I
.'
mm.•..• --
õmirl•_
-0.4
15mi•----•"'•
\ •4 mirt
0.5
8 mi
o7•
•N 0m.i,•
0.s•z
8mln
0,9
•
1.0
1,1
1.2
1,3
1.4
1,5
3 0 350 3
WAVELENGTH (millimicrons)
__ _ H•o/OxH'
H,,O,,
+ HO,- • ßH20 +OH-
[ .4' decomposition +0,2
884 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS
I I I]
24.(
20.,
x 16.•
i
r.
.--
12.0
.--
:3
©
'• 8.0 ©
._•
4.0
1 2 3
Table III
Physicochemical
Propertiesof SolubilizedMelanin
Solubilizationof melanin by dilute solutionsof H•O,., presented
itself as a potentially very useful tool for better characterizationof this
intractable polymer, provided that the modificationbrought about by
the peroxideattackwasnot too great. It wasthoughtlikely that under
mild conditions of treatment the primary reaction would be the
elimination of the solubility-restrainingcross links and the overall
chemicalnature of the pigment would be retained. Solubilizedmelanin
wasthereforeprepared,and someof its propertieswere examinedand
comparedto thoseof intact melanin,where possible.
Solubilization of the granules was effected at low concentrationsof
H..,O2(1%) in 0.5:1I ammonia at pH 10 and 200:1 liquor ratio.
Complete dissolutionof melanin under these conditionstook place
within 60 min. At this point the peroxidewasdestroyedby platinum
black, the water wasremovedby evaporationon a steambath, and the
product was isolatedas a water-soluble,highly lustrousmaterial. On
acidificationto pH 2, the solubilizedmelanin precipitated. This prod-
uct wasdenotedas melanin free acid (MFA). Its solubility behavior is
typical of a polymer containingfew ionizablegroups,dissociationof
which forcesthe polymeric chain into solution. Thus MFA remains in-
solubleat low pH and dissolves rapidly when the pH of the systemis
raised above 4.
0.4
0.5
0.6 •>
I).7•
11.8
•
z
0.9m
ø
1.0
1.2
1.3
1.4
200 f • • • •i
2 0 • • I I I
300 • f, 1.5
WAVELENGTH (millimicrons)
Table IV
Table V
Table VI
Cysteicacid 55 289
Asparticacid 455 447
Threonine 653 642
Serine 870 820
Glutamic acid 871 868
Proline 672 700
Glycine 539 525
Alanine 471 460
• cystine 1380 1130
Valine 538 542
Isoleucine 250 247
Leucine 554 530
Tyrosine 132 120
Phenylalanine 130 119
Lysine 213 225
Histidine 63 69
Ammonia 780 870
Arginine 512 540
Table VII
Swellingof BleachedHair
Of the manywaysin whichtheoxidativedamageof keratinattendant
upon bleachingmanifestsitself (deteriorationof tactile properties,me-
chanicalweakeningof the fiber, increasein alkali solubility,etc.), the in-
creasein swelling representsa convenientmeansfor the assessment of
the extent of damage. This increasein swelling is brought about by
changesin the bulk of the fiber, and thus is directly related to the over-
all chemicalmodificationof keratin by H,•O_o.
Evidencehasbeen presentedhere that of all the amino acidspresent
in keratin, only the cystineundergoesa measurableextent of reaction
with the peroxide;possiblythe oxidativebreakdownof disulfidebonds
alone would satisfactorilyaccountfor the increasedswelling. However,
the principallocusof the bleachingreaction,aswe havelearnedearlier,
is the melanin granule. It is conceivablethat the oxidative destruction
of the •nelanin granulesmight result in formation of discretevoidswith-
894 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS
in the fiber structure. It was thought that the contribution of this fac-
tor to the total swelling characteristicsof the bleached hair could be as-
certainedby specificoxidation of cystincin brown hair with peracetic
acid (without attacking the melanin) or by control bleachingruns on
white hair.
Table VIII correlatesthe swellingdata with the extent of disulfide
bondbreakdown. The swellingwasmeasuredat pH 7 usingthe liquid
retentionmethodwith the reduction-oxidationcycle.
Table VIII
At the same levels of disulfide bond oxidation the bleached brown hair
appearsto be more damagedthan its white counterpart. This difference
could be due to the breakdownof melanin, a contentionsupportedby
the fact that the damagein brown hair can be lowered when the disinte-
grationof pigmentis prevented(peraceticacid oxidation).
It is, however, obvious that the main source of damage residesin
the destructionof disulfidebondswhich not only opensthe structureof
hair but providesadditional hydrophilic centersin the form of cysteic
acid residues. The introductionof theseresiduessignificantlyaltersthe
swellingcharacteristicof hair as illustrated in Fig. 5. A novel feature
of the swellingbehavioris its unusualdependenceupon pH. A pre-
cipitousincreasein swellingof bleachedhair occursin the pH region
5-7.5, while no suchchangeis observedin caseof untreated hair. This
phenomenoncan be bestexplainedby acceptingthe chargerearrange-
ment mechanismpostulated for oxidized wool by Thompson and
O'Donnell (31). The stronglyacidic c¾steicacid residuesare, in the
courseof their formation, being cmnpensatedfor by the ionized basic
groupsof the keratin. As a result, the carboxylicgroupsof the acidic
side chains are being expelled from their salt links and remain essen-
tially un-ionized at pH 4 and below. This decreasein their acidity
HAIR BLEACHING 895
.• 46
Table IX
MechanicalPropertiesof BleachedHair
The disulfidebondscontribute greatly to the wet strengthof keratin
fibers,which decreases almostlinearly with the cystinecontent. On the
other hand, the strengthof the dry fibersis not appreciablyaffectedby
the breakdown of covalentcrosslinks, being dependentlargely on the
main chain length and interchain hydrogenbonding.
When viewed from this standpoint,the changesin mechanicalproper-
ties of hair keratin brought about by bleachingcan be satisfactorilyin-
terpreted in terms of the oxidative attack on the disulfide bondsalone.
Thus, we observe(Table IX) a steadydecreasein wet moduluswith in-
creasedtime of bleachingand virtually no changein either the modulus
or ultimate strengthof dry fibers. The latter observationsupportsthe
view that the extent of the main chain scissionduring the bleaching
processis negligible;it wasshownby Elod (32) that the breakdownof
1% of the peptidebondsin keratin bringsabout an almost20% lossin
the dry strengthof the fiber.
The dry breaking extensionis slightly affectedby bleaching. Cer-
tainly, no evidenceof the brittlenessoften referred to is found. This is
not changedby varyingthe rate of strainingfrom 1 to 50 in./min.
The apparentretentionof dry strengthby the bleachedfibersdoesnot
result from a decreasein regain. On the contrary, the regain of the
fiber increaseswith th? extent of bleaching(Table X) over a wide range
of tested humidities. Bearing in mind the charge rearrangement in-
volving the cysteicand carboxylicacid residues,it would appear that
this increasein regain may be directly related to the ionization of the
HAIR BLEACHING 897
Table X
0.8
• oxidized
0.7
_:
o.6
F--
0.5
I
0.4
0.3
0.0 • 2I 3I 4I 5I 6I 7I 8I
pH
carboxyl
sidechainsto ionize,the regionof theirmechanical
stabili'ty
staysalmostunchangedup to pH 8. This is not so under acidiccon-
ditionswherereducedfibersshowa precipitousfall in yield force.. It is
obvious that the combination of the disulfide bond breakdown and elimi-
nation of electrostatic cross links have a disastrous effect on mechanical
performanceof the fiber. Althoughbleachedhair alsoshowssomeweak-
ening (apparentlya sizeablefraction of acid-labile,salt links is still
present),
thestabilizing
effect
of newelectrostatic
bonds,
involving
•he
cysteicacidresiduesand the chargedbasicgroupsof arginine and lysine
is prominently evident.
ACKNOWLEDGEMENTS
REFERENCES
(13) Zahn, H., Chemical processesduring the bleaching of wool and human hair with
hydrogenperoxide and peroxy acids,J. Soc.Cosmet.Chem., 17, 687 (1966).
(14) Miro, P., Destructionof the tryptophaneof wool by oxidationwith hydrogenperoxide,
Bull. Inst. Text. Ft., 17, 1165 (1963).
(15) Ziegler, K., Wool bleaching, Text.-Prax., 17, 376 (1962).
(16) Piattelli, M., and Nicolaus, R. A., Structure of mclanins and melanogenesis. Structure
of melanin in Sepia, Tetrahedron, 15• 66 (1961).
(17) Nicolaus, R. A., Piattelli, M., and Fattorusso, E., The structure of melanins and
melanogenesis, Ibid., 20• 1163 (1964).
(18) Raper, H. S., The tyrosinase-tyrosine reaction,Blochem.J., 24• 239 (1930).
(19) Green,D. B., and Happey, F., The infra-red spectraof melanins,Cirtel, 1, 283 (1965).
(20) Laxer, G., Somepropertiesof pigmentedanimal fiberswith specialreferenceto bleach-
ing, Ph.D. Thesis, Universityof Leeds,England, 1955.
(21) Valko, E. I., and Barnett G., A study of the swelling of hair in mixed aqueoussolvents,
.l. Soc.Cosmet.Chem., 3, 108 (1952).
(22) Stahl, E., Thin Layer Chromatography,AcademicPress,New York, 1965.
(23) Harris, M., and Br•wn, A. E., Bleaching of keratinous fibrous material. U.S. Patent
2,914,374 (1959).
(24) Swift, J. A., cited from discussion following the presentationof Green'spaper; Cirtel, 1•
300 (1965).
Duke, F. R., and Haas, T. W., The homogeneousbase-catalyzeddecotnpositionof
hydrogenperoxide,J. Phys. Chem.,65• 304 (1961).
(26) Btdl, H. B., Osmoticpressureof egg albumin solutions,J. Biol. Chem., 1•7• 143 (1941).
(27) Burk, N. F., and Greenberg, D. M., The physical chemistry of the proteins in non-
aqueousand mixed solvents. I. The state of aggregationof certain proteins in urea-
water solution,Ibid., 87, 197 (1930).
(28) Everett, A. J., and Minkoff, G. J., Dissociationconstantsof some alkyl and acyl
hydroperoxides,Trans Faraday Soc.,49, 410 (1953).
(29) Perkin, W. H., Someexperimentson the oxidizing action of hydrogenperoxide, Proc.
Chem. Soc.,London, 23• 166 (1907).
(30) Binns,F., and Swan,G. A., Oxidation of somesyntheticmelanins,Chem. Ind. (London),
1957• 397.
Thompson, E. O. P., and O'Donnell, I. J., Comparison of the completenessof oxida-
tion with peraceticacid and performic acid, Aust. J. Biol. Sci., 12, 490 (1959).
Elod, E.. Nowotny, H., and Zahn, H., The structureand reactivity of wool, Kolloid-Z.,
9.•, 50 (1940).