Colloids and Surfaces B: Biointerfaces 41 (2005) 7–14

Hair protein removal by sodium dodecyl sulfate

Rita de Cássia Comis Wagner, Inés Joekes∗
Departamento de Fı́sico-Quı́mica, Instituto de Quı́mica, Universidade Estadual de Campinas, UNICAMP, C.P. 6154, 13084-971 Campinas, SP, Brazil

Received 15 September 2004; received in revised form 16 October 2004; accepted 18 October 2004
Available online 28 November 2004

Abstract

The effect of sodium dodecyl sulfate (SDS) on protein loss was studied. Three kinds of human hair were tested by rubbing or immersion in
water or immersion in SDS solution, at 25, 40 and 70 ◦ C. Under friction, hair treated with SDS solution loses seven times more protein than
in water, while by immersion, protein loss is roughly two times higher in SDS than in water. Protein loss increases at higher temperatures.
Estimated activation energy values for protein loss by immersion are 69 ± 22 kJ mol−1 for blended brown hair; 40 ± 12 kJ mol−1 for blond
hair (tip-end region) and 61 ± 4 kJ mol−1 for blond hair (root-end region) for samples treated in water, while 53 ± 8, 7 ± 5 and 32 ± 8 kJ mol−1
were the corresponding activation energy values for samples treated in 5% SDS solution. These values indicate that protein loss is mainly a
diffusion-controlled process. The more damaged the hair, the lower the activation energy and the higher the protein loss. From these data, it
can be estimated that daily care shampooing at room temperature will cause opacity and combing difficulties in 1 year and split ends after 3
years by removal of all cuticle layers.
© 2004 Elsevier B.V. All rights reserved.

Keywords: Hair degradation; Shampooing; Color changes; Activation energy

1. Introduction non-keratinous material (3% w/w cystine) such as proteins,

Human hair is composed mainly of ␣-keratin (∼80%
w/w) and so-called non-keratinous materials. Keratin is an ␣-
helical protein with high cystine content [1–3]. If damaged,
no chemical or physical treatment can bring it back to its
original form. This is the reason why cosmetic hair science
is focused on preventing, qualifying and quantifying dam-
ages to human hair. Morphologically, human hair is divided
into three or even four units: cortex, cuticle, intercellular ma-
terial and, sometimes, medulla. The structure and chemical
composition of these units have been extensively discussed
[4–6].
The cuticle has an amorphous character. Each cuticle is
formed by four subunits that have distinct chemical com-
position and reactivity. The A-layer and the exocuticle have
higher cystine content (30% and 15% w/w, respectively) and
a hydrophobic character [2,7]. The endocuticle is made up of
∗ Corresponding author. Tel.: +55 19 37883094; fax: +55 19 37883094.
E-mail address: ines@iqm.unicamp.br (I. Joekes).
enzymes, vitamins, ions, nucleic acids, sugars, carbohydrates
and fatty acids, which are water soluble for the most part. The
endocuticle has a hydrophilic character and a low chemical
resistance when compared with the other cuticle structures
[7,8]. The last subunit is the epicuticle, a thin hydrophobic
layer (2.5 nm) that involves the cuticle, composed mainly of
18-methylenicosanoic acid bonded to a proteolipidic mem-
brane that is also rich in cystine (12% w/w) [2,8]. The cellular
membrane complex (cmc), which is found between the cuti-
cles, is a hydrophilic material rich in polar amino acids and
lysine (2% w/w cystine) [9,10]. It is believed that cmc and
endocuticle are the main diffusion pathways into human hair
[2].
Anionic surfactants are extensively used in detergent for-
mulations as shampoos. It is well known that shampoos cause
hair drying, opacity and difficulty in handling [11]. Polano
[12] links the use of detergents to skin eczema produced by
amino acid solution. In another work, Imokawa et al. [13]
relate skin roughness caused by surfactants with protein de-
naturation through serum bovine albumin (SBA) denaturation

0927-7765/$ – see front matter © 2004 Elsevier B.V. All rights reserved.
doi:10.1016/j.colsurfb.2004.10.023
8 R. de Cássia Comis Wagner, I. Joekes / Colloids and Surfaces B: Biointerfaces 41 (2005) 7–14
potential. Clarkson et al. [14] show the denaturation of many
types of proteins during foaming processes.
Because the surfactant can bind to specific active sites on
the protein sequence, as the positively charged glycine for
instance, promoting its denaturation [15,16], the purpose of
this work is to extend and deepen the knowledge of damage
to human hair caused by surfactants, using sodium dodecyl
sulfate (SDS) as the model compound.
2. Materials and methods
2.1. Samples
Hair samples were (a) a single head Caucasian dark-brown
hair tress, 15 cm in length with uniform color and luster ob-
tained from a donor, (b) the root-end region (8 cm length) cut
from a blended Caucasian dark-brown hair tress with 26 cm
length, purchased from De Meo Brothers Inc., New York,
USA, and (c) a Caucasian blended blond hair tress (con-
tributed by Natura Cosméticos S.A., which was purchased
from De Meo Brothers Inc.), 20 cm long, cut into two sec-
tions (root-end and tip-end).
These tresses were separated into 2 g samples, cleansed
by an 8 h Soxhlet extraction with diethyl ether, dried for 24 h
at room conditions and stored at a controlled 50% RH room.
2.2. Treatments
2.2.1. Immersion washings
Duplicate 1.0 g samples were immersed in 50 mL Erlen-
meyer flasks containing 5 mL of water, 5% SDS (w/v) so-
lution or SDS 5% + 0.5% silicone microemulsion (w/v) (GE
Silicone SM 2115 from Cosmotec® ) solution. After 1 h, the
hair samples were taken out and the protein in the solutions
was quantified. This procedure was repeated for different
times at 4, 25, 40 and 70 ◦ C with sample a and at 0, 25 and
70 ◦ C with samples b and c. The SDS concentration chosen
is expected to simulate that resulting from the addition of
shampoo in a wet one-head hair during daily washings.
2.2.2. Rubbing washings
Duplicate 1.0 g samples were shampooed as follows: (a)
the tresses were wet in a 250 mL Erlenmeyer containing
100 mL of distilled water; (b) the excess water was taken
off; (c) 0.5 mL of water or 10% SDS solution was added; (d)
hair was hand rubbed for foaming; (e) then it was shaken in
water for a few seconds. Protein content in the rinse water
was measured after up to 120 cycles. The SDS concentration
chosen is near to that found in ordinary shampoo formula-
tions.
2.3. The Lowry method to quantify protein loss
Vigorous shaking of hair in the presence of a liquid can
be used to separate cuticles from the cortex [17]. The Lowry
method [18] has been used to quantify damage to human
hair after vigorous shaking in water and in surfactant solu-
tions; the more damaged the fiber, the greater the protein loss
[19,20]. Protein values are considered relative, since the an-
alytical curve is constructed with the absorbance values for
SBA. The method is more sensitive to cystine, cysteine, his-
tidine, tryptophan and tyrosine than to the other amino acids.
Since 23% (w/w) of SBA is composed of these amino acids,
compared to 20–25% (w/w) in human hair, our measurements
of protein loss are very similar to the absolute values.
2.4. Color measurements
Changes in hair color were measured by DRS in a Gretag
Macbeth Color-Eye 2180 spectrophotometer, as explained
elsewhere [21]. The equipment scans a spectral range from
360 to 750 nm in 10 nm steps. The instrument operation con-
ditions were (a) configuration CRIIS (C, ceramic calibration;
R, reflectance; I, ultra-violet frequencies included; I, specular
component included; S, short viewing aperture), (b) D65 il-
luminant, (c) 10◦ viewing angle, (d) sample holder for fibers,
(e) internal reference, and (e) CIELAB equations. The equip-
ment software rendered CIELAB values of L* (lightness), a*
(red/green color axis), and b* (yellow/blue color axis). From
these values, and following ASTM D 22440-85, the calcu-
lated color difference parameters were DL* (lighter if pos-
itive, darker if negative), Da* (redder if positive, greener if
negative), Db* (yellowier if positive, bluer if negative) and
DE* (total color difference, the square root average of the
sum of the squares of Da* , Db* and DL* ). Measurements
were done in sets of 10 readings in the middle of the hair
samples, turning the samples in the equipment holder. DE*
values are significant if higher than 1.0 [21]. Prior to the mea-
surements, the samples were dried with a hair dryer (cold air)
and left standing for 24 h in a 50% UR-controlled room.
2.5. Scanning electron microscopy (SEM)
Scanning electron microscopy (SEM) images were ob-
tained in a Jeol JSM 840A, at 25 kV. Hair segments were
mounted in proper stubs using a double face tape and a cop-
per adhesive ribbon and sputtered with a thin layer of gold.
For each sample, five fibers from each treatment were ob-
served by SEM. The micrographs shown are representative
for each treatment.
3. Results and discussion
3.1. Protein loss by immersion
Protein loss as a function of temperature for samples a
and b is shown in Figs. 1 and 2. As expected, protein loss
increases with temperature [20].
Comparison between the amounts of protein lost shows
that protein loss is less in the blended hair than in the single
 R. de Cássia Comis Wagner, I. Joekes / Colloids and Surfaces B: Biointerfaces 41 (2005) 7–14
Fig. 1. Protein loss (mg g−1 ) for (single head) dark-brown hair immersed in
water (䊉) and 5% SDS solution (). (A) 250 h, 4 ◦ C; (B) 320 h, 25 ◦ C; (C)
130 h, 40 ◦ C; (D) 79 h, 70 ◦ C.
head sample, probably because of the fact that sample was
less damaged from the beginning.
The addition of silicone has no effect on protein loss
caused by SDS. The values are almost the same. Thus, the
experiment was repeated with two regions of the same sam-
Fig. 2. Protein loss (mg g−1 ) for blended dark-brown hair immersed for 84 h
in water (䊉), 5% SDS solution () and 5% SDS + 0.5% SM 2115 solution
(+). (A) 25 ◦ C; (B) 40 ◦ C; (C) 70 ◦ C.
9
Fig. 3. Protein loss (mg g−1 ) for blended blond hair (tip-end) immersed for
84 h in water (䊉) and 5% SDS solution (). (A) 25 ◦ C; (B) 40 ◦ C; (C)
70 ◦ C.
ple, the root and the tip-end of a blond hair, as shown in
Figs. 3 and 4. The addition of silicone again had no effect
on protein loss. As expected, since the tip-end is more dam-
aged than the root-end, protein loss from the root-end region
is lower [23]. Since this is a blended hair, the difference in
Fig. 4. Protein loss (mg g−1 ) for blended blond hair (root-end) immersed
for 84 h in water (䊉), 5% SDS solution () and 5% SDS + 0.5% SM 2115
solution (+). (A) 25 ◦ C; (B) 40 ◦ C; (C) 70 ◦ C.
10 R. de Cássia Comis Wagner, I. Joekes / Colloids and Surfaces B: Biointerfaces 41 (2005) 7–14

preservation conditions between root and tip regions is only
due to soft treatments such as shampooing, combing, expo-
sure to sunlight and the environment. Therefore, the method
is sensitive to these small damages.
No plateau is observed in any curve. Even after 84 h
of treatment (equivalent to 336 daily baths for 15 min) ex-
tractable substances remain in the fibers. The maximum pro-
tein loss is observed for the single head hair treated with 5%
SDS solution at 70 ◦ C, 12.5 mg g−1 or 1.25% of its total mass.
Considering that human hair grows ∼15 cm/year, a protein
loss of about 4% can be projected after 1 year. This is not
enough to remove all the cuticles from the surface, but it is
enough to promote dryness, opacity and resistance to comb-
ing.
3.2. Protein loss by rubbing washings
iments. This could arise from the fact that SDS, by removing
sebum and lipids, increases the friction coefficient of the fiber,
which becomes more damaged by rubbing one fiber against
another than when the process is carried out in water.
3.3. Activation energy
From the protein loss values obtained after immersion,
the damages induced are restricted most probably to cmc and
endocuticle, suggesting that this is a diffusion-controlled pro-
cess. This may be confirmed by the activation energy values,
which were estimated from the isotherms. The reaction order
was estimated using Eq. (1) [24]:
dA
= −kA An (1)
dt

Daily shampooing is not done in the ‘static’ conditions of where dA/dt is the rate of protein loss, kA the rate constant, A
the above experiments. It involves rubbing one fiber against an intermediate concentration and n the reaction order. After
each other for foaming, drying with a towel or a hair dryer, taking logarithms, a linear graph of ln(−dA/dt) versus ln A
brushing and combing. Damages induced by these abrasive is obtained, where n is the angular coefficient and ln k the
actions must be taken into account. Fig. 5 shows the protein linear coefficient. Values calculated in this way are shown in
loss for (single head) dark-brown hair rubbed with 10% SDS Table 1. Note that the relative reaction order decreases with
solution and a control sample, rubbed with water. Protein temperature and is similar for water-treated and SDS-treated
loss continues after 120 treatment cycles, and SDS causes a hair in all cases. This indicates that SDS and water extract
seven-fold greater protein loss than just water. Considering the same substances from the fiber.
that cuticles plus cmc correspond to ∼12% of the entire fiber Using the rate constants in Table 1 and the Arrhenius equa-
mass, a mass loss of 3.5% means that a large portion of the tion (2) [25]
cuticular layer was removed from the fiber surface. This will Ea
cause decreased mechanical resistance and split ends. Conse- ln k = ln A − (2)
RT
quently, just shampooing for a long time is enough to destroy
activation energies were obtained by plotting ln k versus 1/T,
the fiber. Gradually, it will remove the intercellular matter
as shown in Table 2.
and the fibrils will unbind.
The values obtained are in the range of those expected for
As in the immersion experiments, the presence of the sur-
diffusion-controlled processes [2,26]. According to Kubisz
factant contributes to a greater protein loss. However, protein
and Marzec the activation energy for keratin denaturation is
loss during rubbing in the presence of SDS is much greater
above 100 kJ mol−1 [27], and according to McMullen and Ja-
than in the presence of water. Although the SDS concentra-
chowicz [28] the activation energy for tryptophan decompo-
tion is twice as high in the rubbing experiments, protein loss
sition is about 26 kJ mol−1 . These data indicates that keratin
is as much as seven times higher than in the immersion exper-
Table 1
Apparent reaction order for the protein loss isotherms
Temperature Blended Blond, tip-end Blond, root-end
(◦ C) dark-brown
Water
25 0.4 ± 0.2 2.5 ± 0.8 2.6 ± 0.7
2.6 ± 0.5 2.6 ± 0.8
40 2.0 ± 0.3 2.2 ± 0.3 2.2 ± 0.6
2.1 ± 0.4 2.6 ± 0.6 2.1 ± 0.5
70 1.4 ± 0.3 1.4 ± 0.3 1.7 ± 0.2
0.7 ± 0.1 1.3 ± 0.2 1.8 ± 0.1
SDS 5%
25 1.6 ± 0.2 3.3 ± 0.5 2.8 ± 0.7
3.3 ± 0.6 2.7 ± 0.7
40 2.3 ± 0.4 2.35 ± 0.48 2.73 ± 0.48
3.2 ± 0.4 2.55 ± 0.46 2.82 ± 0.42
70 0.7 ± 0.3 1.1 ± 0.2 1.4 ± 0.1
Fig. 5. Protein loss for (single head) blended dark-brown hair treated under 1.0 ± 0.2 1.1 ± 0.2 1.5 ± 0.1
friction with water (䊉) and SDS 10% () for up to 120 times. T ∼ =25 ◦ C.
 R. de Cássia Comis Wagner, I. Joekes / Colloids and Surfaces B: Biointerfaces 41 (2005) 7–14 11

Table 2
Estimated activation energy for the protein loss of human hair when im-
mersed in water and SDS 5% for 84 h
Ea (kJ mol−1 )

Blended dark-brown Blond, tip-end Blond, root-end

Water 70 ± 22 40 ± 12 61 ± 4
SDS 5% 53 ± 8 7±5 32 ± 8

was not denaturated in our experiments, although some tryp-

tophan could have been decomposed. The estimated activa-
tion energy in water is about twice that in SDS solution for
the root-end region of the blended blond hair and 5.7 times
larger for the tip-end region; for the blended dark-brown hair,
a small difference of 1.3 is found. The sample that shows the
larger protein loss has the lower activation energy. Thus, SDS
may increase the hydrophilic character of the fiber, interacting
with structural lipids at neutral pH, allowing an easier water
extraction of proteinaceous matter. Damages in the cmc and
endocuticle facilitate the removal of cuticles, as shown by
Scanavez et al. [22]. These authors observed the formation
of holes in the cmc and in the endocuticle and proposed that
the cuticle detaches through those subunits.
3.4. Color changes induced by protein loss
The solutions obtained in the immersion experiments have
a light brown color. Since no hair protein is optically active
in the visible region of the electromagnetic spectrum, col-
oration is unexpected. Melanin extraction can happen only
if the cortex has been severely damaged. On the other hand,
tryptophan can change hair color if damaged [28].
The color properties of the immersed hair samples were
measured before and after treatment. Results are shown in box
plots, in Figs. 6–8. All samples show small color changes. The
Fig. 7. Box plots of 20 (10 per duplicate) measurements of the color param-
eters of blended blond hair (tip-end) immersed for 84 h in water at 25 ◦ C
(W25), 40 ◦ C (W40) and 70 ◦ C (W70) and in 5% SDS solution at 25 ◦ C
(SDS25), 40 ◦ C (SDS40) and at 70 ◦ C (SDS70).
blended dark-brown hair is lighter, redder and yellowier after
the treatments, and these tendencies increase with increasing
temperature. DL* is the main contributor to the total color
change (DE* ), which means that damage caused by protein
loss is soft. The presence of the silicone in the SDS solution
causes no effect on color, which agrees with the protein loss
data. The tip-end of the blended blond hair is also yellowier
after the treatments, but darker after being treated with water
and lighter after being treated with SDS solution and tends
to be redder only after being treated with water. In this case,
temperature seems to have no effect on color changes. How-
ever, for the root-end of the blended blond hair, an effect of
temperature on lightness is observed, as shown in Fig. 8. At
25 ◦ C the hair is lighter after treatment with SDS but gets
darker with the increase in temperature.

Fig. 6. Box plots of 20 measurements (10 per duplicate) of the color param-
eters of blended dark-brown hair immersed for 84 h in water at 40 ◦ C (W40) Fig. 8. Temperature influence in the lightness parameter DL* of blended
and 70 ◦ C (W70), in 5% SDS solution at 40 ◦ C (SDS40) and 70 ◦ C (SDS70) blond hair (root-end) (duplicate) immersed for 84 h in 5% SDS solution at
and 5% SDS + 0.5% SM 2115 solution at 40 ◦ C (Si40) and at 70◦ (Si70). 25 ◦ C (SDS25), 40 ◦ C (SDS40) and 70 ◦ C (SDS70).
12 R. de Cássia Comis Wagner, I. Joekes / Colloids and Surfaces B: Biointerfaces 41 (2005) 7–14
Fig. 9. SEM micrograph of the reference blended blond hair (root-end re-
gion) showing hair topography before treatment. Notice the presence of
rough regions (*).
Well-preserved samples become darker after immersion in
water, as proposed by Scanavez et al. [22]. During the clean-
ing of the hair with ether, holes are formed or enlarged in
the endocuticle. Water fills these cavities facilitating a repo-
sitioning of the amorphous proteinaceous materials, which
makes the fibers darker. The more damaged the fiber, the less
extractable material is present in the cuticles, and damages
begin to appear in the cortex. When the cortex is damaged,
Fig. 10. SEM micrographs of blended blond hair fibers (root-end region)
after being immersed in water for 84 h at 25 ◦ C (A) and at 70 ◦ C (B). Both
have a dirty appearance and micrograph B shows more cracks and fissures
(*) on cuticles than A.
changes in the Da* and Db* values are expected, but L* values
are roughly unchanged since cuticle damage is maximum and
since holes formed in the cortex are fewer. So, from the light-
ening observed, SDS does not damage significantly the cor-
tex, although extracting more proteinaceous materials than
water.
Temperature should change the color of well-preserved
fibers more than the color of damaged fibers. This was ob-
served in every case, except for the root-end region of the
blended blond hair immersed in SDS, which became darker
at higher temperatures. Since it is expected that, initially,
SDS facilitates the rearrangement of the amorphous mate-
rials inside the holes, it is possible that the treatment time
was insufficient to remove all the extractable proteinaceous
material.
3.5. Surface changes induced by protein loss
Fig. 9 shows a SEM micrograph of the blended blond hair
(root-end region). The hair surface shows the typical features
described by other authors [22]. The reference fiber shows
some eroded regions and cracks, probably caused by daily
care. Cuticular cells exhibit irregular contours as if broken
edge parts had been removed. Rough regions may be noticed
as a result of cuticle detachment through endocuticle or cmc
[22].
Fig. 11. SEM micrographs of blended blond hair fibers (root-end region)
immersed in 5% SDS solution (w/v) for 84 h at 25 ◦ C (A) and at 70 ◦ C (B).
Both show a clean appearance. Cracks in B reach several cuticles (*) and
surface porosity is higher than in A.
 R. de Cássia Comis Wagner, I. Joekes / Colloids and Surfaces B: Biointerfaces 41 (2005) 7–14
Fig. 10 shows SEM micrographs of the blended blond
hair (root-end region) after immersion in water at 25 and
70 ◦ C. Comparison with the reference hair shows increase
of roughness surrounding cuticle borders, conferring a dirty
appearance to the fiber (Fig. 10A). These regions do not look
like endocuticle or cmc. Temperature increases induce crack
propagation on the fiber surface (Fig. 10B).
Fig. 11 shows the sample immersed for 84 h in 5% SDS so-
lution at 25 ◦ C (A) and 70 ◦ C (B). Roughness disappears, and
the cuticles show angulated borders. This renders a cleaner
appearance, which is consistent with the darkening obtained
in the color data. The greater protein loss in SDS-treated
samples could arise from this surrounding material being re-
moved by the surfactant. The increase of temperature to 70 ◦ C
causes more damages to the fibers; cracks penetrate through
several cuticles as observed in Fig. 11B.
Fig. 12 shows the reference single head dark-brown hair
(A). This hair sample seems better preserved than blended
blond hair. The scales have a smoother surface. In Fig. 12B,
a fiber exposed to 120 water treatment cycles in a rubbing
experiment is shown. A rough surface can be observed. In
Fig. 12C, a fiber exposed to 120 washing cycles with 10%
Fig. 12. SEM micrograph of reference single head brown hair (A), the sur-
face of a fiber treated in water (B) and a fiber treated in 10% SDS solution
(w/v) in rubbing experiments (C), showing exposed endocuticle or cmc re-
gions (*).
13
SDS solution (w/v) in the same experiment is shown. Some
rough regions are identified as the endocuticle or cmc [22],
which means that cuticles were detached from hair surface. It
may be the reason for the greater protein loss obtained. This
was not observed in the immersed samples. While immer-
sion dissolves some intercellular material and endocuticle,
rubbing causes more damages as cuticles detach due to a
physical process.
4. Conclusions
Protein loss data shows that human hair immersed in water
loses less protein than in 5% SDS solution, by about half.
This difference increases with increasing temperature. No
plateau was observed in the isotherms, which indicates that
protein loss could continue until the entire degradation of
the fiber. Initial preservation of the hair influences protein
loss, which is higher when hair is more damaged. The values
found are very close to absolute values and indicate that the
damage was restricted to the cuticles. SEM images indicate
that rubbing hair is responsible for the major protein loss
during daily shampooing, causing cuticle detachment in a
physical process. Immersion promotes a chemical process of
proteinaceus structure dissolution and also damaging.
There were some small changes in color. The silicone
added to the SDS solution showed no effect on protein loss or
the color changes caused by SDS. The estimated activation
energy values were greater for water treatment than for SDS.
According to the range found, 7–70 kJ mol−1 , protein loss is
controlled by diffusion through the fiber.
Altogether, to evaluate cosmetic treatments on human hair
through protein loss measurements it is necessary to con-
sider the preservation conditions of the fiber. It cannot be
done on only one type of hair, since cosmetic treatments
could generate different effects on hair with different lev-
els of damage. The preservation conditions are intimately
related with the chemical properties of the fiber, such as the
hydrophilic/hydrophobic character. Thus, it is necessary to
obtain adequate controls.
Acknowledgments
The authors acknowledge financial support of FAPESP
(Grant 01/14161-9) and CNPq (Grant 133215/2001-6).
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