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Prevention of hair surface aging

Article  in  Journal of Cosmetic Science · June 2011

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Prevention of Hair Surface Aging
Erik Schulze zur Wiesche1, Andrea Körner2,Karola Schäfer2, Franz-Josef Wortmann3
1
Henkel AG & Co. KGaA, Hohenzollernring 127-129, 22763 Hamburg, Germany
2
DWI an der RWTH Aachen e.V., Pauwelsstr. 8, 52056 Aachen, Germany
3
School of Materials, The University of Manchester, Manchester M13 9PL, UK

Synopsis

The hydrophobic character of the surface of human hair is particularly attributed to the lipid

components of the epicuticle and to a layer of covalently bound fatty acids. This outer f-layer mainly

consists of 18-methyl eicosanoic acid (18-MEA), which is covalently bound to the underlying protein

matrix, forming the epicuticle as composite surface structure. Daily weathering and chemical

treatments, specifically oxidative bleaching, decrease the hydrophobicity of the outer hair surface

drastically.

Multiple daily stress, simulated by an automatic test device including shampooing, blow drying and

sun light exposure, changed the lipid composition of hair significantly. A marked loss of 18-MEA was

observed. Decreasing contact angles are the direct consequence. A new method to determine the

“pseudo-static” contact angle on hair was developed. The results correlate with the corresponding

data obtained by dynamic contact angle measurements according to Wilhelmy. Besides that, the

resorption time of water droplets by the hair surface provides additional information about the

intactness of the outer f-Layer.

Specific proteolipids, which are lipid-modified keratins, are able to reconstruct the surface layer of

damaged hair by creating renewed surface hydrophobicity and extending the water resorption time by

the hair surface.

INTRODUCTION

Human hair is protected against extrinsic aging stress by a hydrophobic outer layer. The

intactness of which is essential for the consumer’s perception of healthy and shiny hair (5,6).

This outer layer, generally referred to as epicuticle, is a thin, chemically resistant layer, which

is estimated to contain a high proportion of lipids ranging from approx. 22% up to 44%
depending upon the method of removal and subsequent treatments (17). In addition to

solvent extractable lipids there are furthermore covalently bound lipids at the surface forming

the so called f-layer. It mainly consists of anteiso (+)-18-methyleicosanoic acid (18-MEA),

bound as a thioester (1-3) to the cysteine residues in the underlying protein layer (4). This

arrangement imparts pronounced hydrophobicity to the hair surface, which is in marked

contrast to the overall hydrophilicity of the hair bulk.

Contact angle measurements of undamaged hair, taken near the scalp, show consistently

contact angles with water of 100° -110° (11,14). Due to daily aging and cosmetic influences

the hydrophobicity of the surface decreases. Hydrophilic regions are induced on the fibre

surface through the oxidation of the lipid end groups and the exposure of protein patches.

Thus hydrophilic effects increase along a hair towards the fibre tip due to removal of lipids on

the surface, leading to contact angles typically around 70° or 80° at the fibre tip (14). These

effects are mainly caused by UV light exposure, intensive shampooing, mechanical abrasion

and chemical processes e.g. oxidative bleaching. Oxidative bleaching might decrease the

contact angles even further to values around 40° (10,12).

In order to investigate effects of daily aging on hair more systematically a recently

established multiple day-by-day stress simulation was applied (7). This automatic test device

includes shampooing, blow drying and sun light exposure. The test procedure was carried

out by a robot, which offers a high degree of reproducibility with respect to the induced hair

damage profiles. The impact of different oxidative bleaching treatments was studied in

comparison to the natural aging effects.

The contact angle of hair with water is an excellent parameter to indicate the general

damage constitution of the hair surface. It is easily measurable by means of the dynamic

principle according to Wilhelmy, a broadly published method for the determination of contact

angle on single hair fibres (10-14). Determination of the wettablility of a hair by the Wilhelmy

balance principle involves the measurement of the vertical force on hair fiber when contact

with the liquid is established (14). The forces F are recorded while the fibre is immersed into
the liquid. The contact angle is now accessible by knowing the fiber perimeter L and the

surface tension of water according to

F L LV cos (1)

The resulting microbalance reading F includes the buoyancy force Fb on the fibre, the weight

of the fibre Fg and the wetting force F :

F = F - Fb + Fg (2)

For a single human hair fibre the buoyancy force is negligible versus the wetting force F .

The weight of the hair is zeroed before the hair touches the surface of the liquid. Thus, the

resulting force can be considered as equivalent to the wetting force.

Figure 1. Determination of the dynamic contact angle of single hair fibres in contact with water (13).
F
In addition to the dynamic single fibre approach a new method was developed to determine

the “pseudo static” contact angle formed by water droplets on parallel aligned hair collectives.

In order to reach the “pseudo-static” stage, hair should deliver contact angles above approx.

80°. If contact angles are lower, the water resorption by hair takes place too fast. The shape

of the droplet was recorded from a perpendicular positioned directly after deposition (approx.

1s). The evaluation is based on the asymptotical fitting of a tangent to the segment where the

water contacts hair (Figure 2).

 Hair strand holder

Figure 2. Determination of the “pseudo-static” contact angle of a droplet of water deposited on an

aligned hair strand.

The resorption time of the water droplet by the hair can be considered as an additional

parameter to evaluate the damage degree of the hair surface. Thus the droplet was

monitored over time and the elapsed time until the water was totally resorped by the hair was

determined, as shown in Figure 3. The resorption kinetic differs from a spontaneous

resorption for severely damaged hair to no detectable resorption for virgin hair. Water

droplets remain for hours on virgin hair strands. They slowly shrink with evaporation. In

agreement with these observations medium bleached hair was used for this study. The

determined resorption times ranged from 10 to 100 s.

1s 20 s 25 s

28 s 29 s 30 s

Figure 3. Resorption process of a droplet of water on an aligned hair strand recorded from a

perpendicular camera angle.

RESTORATION OF THE DAMAGED HAIR SURFACE

Objective of this study was to restore the natural properties of the virgin hair surface.

Considering the morphology of the outer hair surface, where lipids are covalently bound to a
protein matrix, lipid-modified proteins, the so called proteolipids, were tested as potential

surface restoring agents.

Assuming that the adhesion and organization of proteolipids on the hair surface is controlled

by electrostatic and polar forces (protein-protein) as well as apolar interactions (hydrophobic

forces), a lipophilic surface layer should be specifically formed, where protein patches are

exposed (Figure 4). The incorporation of proteolipids should increase the hydrophobicity of

damaged hair, leading to higher contact angles.

Figure 4. Schematic diagram of hypothesis of the adhesion principle of proteolipids on damaged hair

surfaces.

MATERIALS

HAIR

For all tests a mixture of light brown Caucasian hair (Color Code 7/0) from Kerling

International Haarfabrik GmbH in Backnang (Germany) was used. The tests were performed

on hair strands (width 4 cm, length 13 cm, weight 250 mg) and on single fibers (length 30

mm).
STANDARD HAIR CLEANSING

An aqueous solution (pH 5.5) of 12.5% (w/v) sodium laureth sulfate was applied on hair (0.25

g / 1 g). The fibres were rubbed against each other for 1 min. Afterwards it was washed out

with tap water at approx. 30 °C for 1 min.

SHAMPOO A

Aqua, sodium laureth sulfate, disodium cocoamphodiacetate, citric acid, sodium chloride,

Sodium Benzoate, salicylic acid.

SHAMPOO B

Aqua, sodium laureth sulfate, disodium cocoamphodiacetate, citric acid, sodium chloride,

sodium benzoate, proteolipid SR, salicylic acid.

PROTEOLIPID SR

All investigations were performed with proteolipid CR which consists of an alkyl chain derived

from coco palm oil (C8-C18), a hydrolysed protein present in wool keratin and a quaternized

adapter group (Cocodimonium hydroxypropyl hydrolyzed keratin). Proteolipid SR is water

soluble.

METHODS

MULTIPLE DAILY STRESS SIMULATION

The stress simulation, consisting of shampooing, drying and sun exposure, was

automatically run by the RV E2 robot from Mitsubishi Electric Corporation, Tokyo (Japan).

Firstly all hair samples were immersed into 160 ml of a solution of shampoo A for 3 min at a

temperature of 38°C. Afterwards the hair samples were removed from the vessel and rinsed

with 20 liter tap water at a temperature of 38°C for 2 min and dried with an air heater (LE

10000S, Leister Process Technologies, Kaegiswil, Switzerland) at 80 °C for 30 min. Sun

exposure was simulated for 60 min at 764 W with an ATLAS Suntest (CPS+, Chicago, USA).

The time for one cycle was approx. 2.5 h. 50 cycles in total are run automatically within 5

days (7).
ULTRA BLEACHING

Hair strands were treated for 45 min with a mixture of 6% hydrogen peroxide (Hyprox 500®,

Evonik) and 3% potassium persulfate (KPS-5®, Evonik) at pH 10. This mixture was spread

by using a brush and washed out with tap water at approx. 30 °C for 3 min.

MEDIUM BLEACHING (I)

Hair strands were treated for 50 min with 7 % hydrogen peroxide (Hyprox 500®, Evonik) at

pH 8.8. This mixture was spread by using a brush and washed out with tap water at approx.

30 °C for 3 min.

MEDIUM BLEACHING (II)

Hair strands were treated for 25 min with 3 % hydrogen peroxide (Hyprox 500®, Evonik) at

pH 9.5. This mixture was spread by using a brush and washed out with tap water at approx.

30 °C for 3 min.

QUANTIFICATION OF COVALENTLY BOUND LIPIDS

The hair samples were subjected to a 16 h extraction chloroform/methanol azeotrope in a

Soxhlet apparatus. Alkaline catalyzed total hydrolysis of the hair material was performed with

2M alcoholic potassium hydroxide solution and the lipids were recovered by repeated hexane

extraction. Aliquots of the lipid extract were reacted with a silylation (MSHFBA, Macherey &

Nagel) reagent to form their trimethylsilylester derivatives and the fatty acids, namely 18-

methylicosanoic acid, were analyzed by gas-liquid chromatography/mass-spectrometry

coupling (GC-MS). Tridecanoic acid was applied as internal standard for quantitative

measurements. Duplicate sub-samples of each lipid extract were prepared and analyzed by

GC-MS.

FLUORESCENCE MICROSCOPY

The fluorescence microscopic investigation was performed with a scanning photometer

microscope MPM03, Zeiss, Jena, Germany). The fluorescence labeling of the proteins was

carried out with fluorescein isothiocyanate (FITC) isomer I (Sigma, St. Louis, USA) (8, 9).
SCANNING FORCE MICROSCOPY

Scanning Force Microscopy (SFM) studies were conducted using a Nanoscope IIIa from

Digital Instruments operating in the tapping mode. Standard silicon cantilevers were used

(PPP-NCH from Nanosensors) with a spring constant k 42 N/m and an oscillation

frequency f0 330 kHz. Height and phase images were recorded simultaneously at a scan

rate of 1 Hz. All measurements were performed at amplitude A0 of the freely oscillating

cantilever of 30 50 nm. Set-point amplitudes Asp were in the range of 0.85 0.95A0 and

0.35 0.45A0, corresponding to light-tapping and hard-tapping conditions, respectively (15).

DYNAMIC CONTACT ANGLE MEASUREMENTS

The determination of the dynamic contact angles was performed by the Tensiometer K14

(Krüss GmbH, Hamburg, Germany). The hair perimeter L was determined by immersing the

hair fiber in n-heptan (99%), which shows total wettability ( =0). Advancing contact angle

was measured in distilled water at 20 °C. The immersion rate was 1mm/min in root-tip

orientation at the maximum immersion depth of 1mm.

PSEUDO-STATIC CONTACT ANGLE MEASUREMENTS AND DETERMINATION OF

DROPLET RESORPTION TIME

A droplet of 25 l of distilled water was placed by using a micro-pipette on a parallel aligned

and fixed hair strand of 2 g weight and 18 cm length. The side of the droplet is recorded by

digital camera (D40 F/3.5-5.6, Nikon co., Japan). Camera perspective is a perpendicular to

the hair fiber axes on level with the hair strand.

RESULTS AND DISCUSSION

AGING OF OUTER HAIR SURFACE

After simulation of approximately 100 Middle European summer days (equivalent to 50

cycles of shampooing, blow drying and sun light exposure) significant changes both in the

lipid composition and in the contact angle were detected. The contact angle dropped from
106° to 68° and the content of 18-MEA decreased by approximately 24 %. The ultra

bleaching process removed significantly more surface lipids and showed smaller contact

angles shown in Figures 5 and 6.

0,30
0.25
0,25
0.19
0,20
mg/ g hair

0.14
0,15

0,10

0,05

0,00
before aging "aged hair" ultra bleached

Figure 5. Amount of 18-MEA extracted from hair before (untreated) and after aging simulation (“aged

hair”) in comparison to the amount of 18-MEA extracted after ultra bleaching (ultra bleached).

140

120 106
Contact angle / °

100

80 68**
60 48**
40

20

0
before aging "aged hair" ultra bleached

Figure 6. Dynamic contact angles determined according to Wilhelmy before (untreated) and after

aging simulation (“aged hair”) in comparison to the contact angle of ultra bleached hair (ultra

bleached) (**p < 0,01 calculated between “before aging” and the samples).

DETECTION OF SURFACE CHANGES RELATED TO PROTEOLIPIDS

A high affinity to the hair surface for the proteolipid SR was confirmed by means of

fluorescence microscopy. Hair was immerged into an aqueous solution of 0.15 % FITC-

labelled proteolipid for 5 min and rinsed out under tap water for 3 min. An intensive and
widespread surface coverage was detected for the ultra bleached hair (Figure 7a). Areas of

cuticle edges show the highest fluorescence intensity. “Aged” hair shows a much more

inhomogeneous light distribution. Here the fluorescence intensity is mainly located at cuticle

edges (Figure 7b). These differences in the fluorescence intensity correspond well to the

obtained differences in contact angles and the 18-MEA losses reported in Figures 5 und 6.

a b

Figure 7. Fluorescence micrograph of ultra bleached (a) and “aged” hair (b) treated (for 5 min) with

FITC-labelled proteolipid SR (0.15%, m/m).

In addition to fluorescence microscopy SFM investigations were performed to visualize the

cuticle surface topography and possible lipid organization at the hair surface before and after

bleaching and after treatment with the lipid-modified keratins respectively. The upper graph

of Figure 8 shows the surface of the virgin hair after cosmetic relevant standard

cleansing; it is covered by a “mosaic structure” formed from stacks and terraces of lipids

showing a well-defined, reproducible height of approximately 3 nm (green arrows in figure

8a) and widths between 20 nm and 70 nm (pink arrows in figure 8a).

Figure 8. SFM images (topography) of virgin hair with cosmetic relevant standard cleansing (a) and of

ultra bleached hair (b).

This nano-scaled lipid multilayer structure is completely removed by oxidative bleaching as

demonstrated in Figure 8b. Instead a surface topography showing streaks oriented parallel to

the longitudinal axis of the hair is observed; a width of approx. 350 nm (in a range between

200 nm and 500 nm) at the basis of the streaks (black arrows in Figure 8b) is determined by

the nanoscope analysis while at their top ends a width of approx. 100 to 200 nm is measured

(pink arrows in Figure 8b). The indentations arranged parallel to the longitudinal fibre axis

have depths of approx. 7 nm to 10 nm (green arrows in Figure 8b); as a consequence of the

high resolution in this study, smaller cavities of approx. 3 nm depths are observed on top of

these striations, some of them round, some more oblong.

The phenomenon of longitudinal “striations” has already been described for mammalian hair

by J. Smith (21) in 1997 and he assigned this “woodgrain appearance” to exocuticle material

exposed after the removal of epicuticle and A-layer due to damaging effects. Later Swift and

Smith (3) detected this striation phenomenon on the outer surface of a wide range of
mammalian keratin fibres afore subjected to a thorough cleansing procedure by either

sonication in sodium dodecyl sulphate or Soxhlet extraction with chloroform/methanol. They

determined the striations “to have a lateral spacing of 350 nm, to be of convex profile, and

rising to a height of approx. 9 nm”. These dimensions fit very well to those detailed above for

the cuticle of bleached hair.

The rinse-off treatment of bleached hair with an aqueous solution of 0.15% proteolipid SR

changes the surface structure of the damaged hair significantly. Figure 9 shows in direct

comparison the SFM images of the virgin hair (a), the ultra bleached hair (b) and the ultra

bleached hair treated with an aqueous solution of proteolipid SR (c). In consequence of the

proteolipid treatment the striations are no longer visible and substituted by patterns which

rather resemble the multi layered structures observed for the virgin hair surface (a).

Figure 9. SFM image (topography) of a) virgin hair, b) ultra bleached hair and c) ultra bleached hair

treated with an aqueous solution of proteolipid SR (0.15%, m/m).

EFFECTS OF PROTEOLIPIDS ON THE PHYSICAL PROPERTIES OF THE HAIR

SURFACE

The effects of proteolipid SR were investigated by means of dynamic contact angle

measurements according to Wilhelmy on ultra damaged hair. The application of a 0.03%

solution of the proteolipid increases the contact angle significantly up to 54°. The effect of

hydrophobization increases linearly with the concentration up to a level of 0.15%. At this

stage a saturation concentration seems to be reached (Figure 10).

Figure 10. Dynamic contact angles of ultra bleached hair and treated hair with different concentrations

of proteolipid SR (*p < 0.05. Numbers indicate references for calculation).

The effect of a rinse-off treatment consisting of an aqueous solution containing 0.15%

proteolipid SR strongly depends on the damage degree of the hair surface, as shown in

Figure 11. The contact angle of ultra bleached hair increases more than 40% (from 48° to

69°). The surface properties of medium bleached hair do not significantly change and the

contact angle of the virgin hair surface slightly decreases. The latter effect may be explained

by hydrophobically controlled surface adhesion of proteolipids at the intact hydrophobic hair

surface.
 110 103
untreated treated
96*
contact angle [°] 100

90
79 80
80
69**
70

60
48
50

40
ultra bleached medium bleached (I) virgin

Figure 11. Dynamic contact angle of ultra bleached, medium bleached and virgin hair before and after

treatment with an aqueous solution of proteolipid SR (0.15%, m/m) (*p < 0.05; **p < 0.01 calculated

“untreated” vs. “treated”, respectively).

Investigations by means of the droplet method delivered similar results for the medium

bleached hair (II) and the virgin hair. No significant difference between the “pseudo-static”

and the “dynamic” contact angle were found for untreated hair. In contrast to the dynamic

contact angle measurements, significant hydrophobization effects for proteolipid SR were

observed even on medium bleached hair by using the pseudo-static contact angle

measurement, as shown in Figure 12. The application of the droplet method on ultra

bleached hair is not feasible due to the quick water resorption by hair.

106

102

98
contact angle / °

94

90

86

82
Mean
Mean+/-Std.Err.
78 Mean+/-1.96*Std.Err.
1 2
medium bleached hair (II) after treatment

Figure 12. Pseudo-static contact angle on medium bleached hair (II) before and after application of

basic shampoo B containing proteolipid SR (0.15%, m/m).

RESORPTION TIME OF WATER BY HAIR

The resorption time of the water droplet by the medium bleached hair (II) before and after the

treatment of a basic shampoo B containing 0.15% proteolipid SR was determined. The

resorption time was significantly extended from 79 s to 140 s (p < 0.05).

200

180

160
resorption time / s

140

120

100

80

60

40 Mean
Mean+/-StdErr.
Mean+/-1,96*Std.Err.
20 re f cro quat

medium bleached hair (II) after treatment

Figure 13. Resorption time of water droplets by medium bleached (II) before and after application of

basic shampoo B containing proteolipid SR (0.15%, m/m).

PREVENTION OF HAIR SURFACE AGING

The multiple usage of shampoo B containing 0.15% proteolipid SR during the simulation of

approximately 100 Middle European summer days reduced the degree of aging damage

significantly. The decrease of the contact angle due to the simulated aging, as shown in

Figure 6, significantly lowers by 11.4 % (p<0.05).

SUMMARY AND CONCLUSIONS

Simulated day-by-day aging causes a significant reduction of the natural hydrophobic

properties of virgin hair. Contact angles strongly decrease due to a significant loss of 18-

MEA. Ultra bleaching shows significantly stronger damage on the hair surface than the

simulated aging. The contact angle of hair with water is an accurate parameter to evaluate
the damage degree of the hair surface and the intactness of the F-layer. Contact angles can

be determined on single hair fibers indirectly by means of dynamic wetting force

measurements according to Wilhelmy and directly by evaluation of water droplets on hair

strands under “pseudo-static” conditions. For the latter approach a new method was

established. The results of this method correlate well for untreated hair to the corresponding

Wilhelmy-data. The determination of the resorption time of the water droplets by hair offers

an additional test parameter to characterize the constitution of the hair surface.

Specific proteolipids, which are lipid modified proteins, show a very high affinity to damaged

areas on the hair surface. This was confirmed by fluorescence microscopy and scanning

force microscopy studies. The distribution strongly depends on the damage degree of outer

hair surface. Due to the high surface deposition on damaged hair, proteolipids are able to

restore the natural hydrophobic properties of virgin hair. This surface restoration leads to an

extended resorption time of water by hair.

Acknowledgements

The authors wish to thank Ahmed Mourran, DWI an der RWTH Aachen, for the performance

of the scanning force microscopy measurements of human hair.

References

(1) A.P Negri, H.J Cornell and D.E. Rivett, A model for the surface of keratin fibres, Text.

Res. J., 63, 109-115, 1993.

(2) L.N. Jones and D.E. Rivett, The role of 18-Methyleicosanoic acid in the structure

and formation of mammalian hair fibres, Micron, 28, No. 6, 469-485, 1997.

(3) J.A. Swift and J.R. Smith, Microcopical investigation on the epicuticle of

mammalian keratin fibres, J. Microscopy, 204,203-211, 2001.

(4) A. Körner, G. Wortmann, Isolation of 18-MEA containing proteolipids from wool

fibre cuticle, Proceedings 11th Int. Wool Textile Res. Conf., Leeds (UK), 4-9

September 2005.
(5) H. Tanamachi, S. Tokunaga, N. Tanji, M. Oguri and S. Inoue, 18-MEA and hair

appearance, J. Cosmet. Sci., 61, 147-160, 2010.

(6) Y. Masukawa, H. Tsujimura, H. Tanamachi, H. Marita and G. Imokawa, Damage

to human hair caused by repeated bleaching combined with daily weathering

during daily life activities, Exog Dermatol, 3, 273-281, 2004.

(7) E. Schulze zur Wiesche, T. Gassenmeier, D. Fischer, E. Poppe, P. Somfleth, K.

Schäfer and A. Körner, Specific repair of aging hair keratin, IFSCC Magazine, 11,

(4) 317-320, 2008.

(8) E.S. Cooperman and V.L. Johnsen, Penetration of protein hydrolysates into

human hair strands, Cosmetic and Perfumery, 88, 19-22, 1973.

(9) R.T. Jones and S.P. Chahal, The use of radio labeling techniques to measure

substantivity to, and penetration into, hair of protein hydrolysates, Internat. J.

Cosmet. Sci., 19, 215-226, 1997.

(10) R. Molina, F. Comelles; M.R. Julia and P. Erra, Chemical modifications on human

hair studied by means of contact angle determination, J. Colloid Interface Sci.,

237, 40-46, 2001.

(11) R.A. Lodge and B. Bushan, Wetting properties of human hair by means of

dynamic contact angle measurements, J. Appl. Polym. Sci., 102, 5255-5265,

2006.

(12) E. Schulze zur Wiesche, Specific characterization of the human hair surface and

influences of cosmetic relevant agents, PhD Thesis, Rheinisch-Westfälische

Technische Hochschule, Aachen, Germany, 1998

(13) F.J. Wortmann, G. Wortmann and E. Schulze zur Wiesche, Spatial Probing of the

Properties of the Human Hair Surface Using Wilhelmy Force Profiles,

Langmuir, 26 (10), 7365–7369, 2010.

(14) Y.K. Kamath, C. J. Dansizer and H.-D. Weigmann, Wettability of keratin fibre

surfaces, J. Soc. Cosmet. Chem., 28, 273-284, 1977.

 (15) S. N Magonov, V. Elings, M.-H. Whangbo, Phase imaging and stiffness in tapping

mode atomic force microscopy, Surf. Sci. Lett., 375, 385, 1997.

(16) J.R. Smith, Use of atomic force microscopy for high-resolution non-invasive

structural studies of human hair, J. Cosm. Cosmet. Chem., 48, 199-208, 1997.

(17) C. M. Carr, I. H. Leaver, A. E. Hughes, Photoelectron Spectroscopy and the

Surface Chemistry of Wool, Text. Res. J., 56, 457, 1986.

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