Impact of protein carbonylation on the chemical characteristics of the hair surface.

Tytuł:: Impact of protein carbonylation on the chemical characteristics of the hair surface.
Autorzy:: Masaki H; CIEL Co., Ltd, Kanagawa, Japan.; School of Bioscience and Biotechnology, Tokyo University of Technology, Tokyo, Japan.
Sinomiya D; School of Bioscience and Biotechnology, Tokyo University of Technology, Tokyo, Japan.
Okano Y; CIEL Co., Ltd, Kanagawa, Japan.; School of Bioscience and Biotechnology, Tokyo University of Technology, Tokyo, Japan.
Yoshida M; School of Bioscience and Biotechnology, Tokyo University of Technology, Tokyo, Japan.
Iwabuchi T; School of Bioscience and Biotechnology, Tokyo University of Technology, Tokyo, Japan.
Źródło:: International journal of cosmetic science [Int J Cosmet Sci] 2021 Dec; Vol. 43 (6), pp. 764-771. Date of Electronic Publication: 2021 Nov 09.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Publication: 2000- : Oxford : Blackwell Science Ltd.
Original Publication: [Oxford, Blackwell Scientific Publications.]
MeSH Terms:: Hydrophobic and Hydrophilic Interactions*
Protein Carbonylation*
Hair/*chemistry
Aldehydes/chemistry ; Humans ; Hydrogen Peroxide/chemistry
References:: Robbins CR. The cell membrane complex: three related but different cellular cohesion components of mammalian hair fibers. J Cosmet Sci. 2009;60(4):437-65.
Molina R, Comelles F, Juliá MR, Erra P. Chemical modifications on human hair studied by means of contact angle determination. J Colloid Interface Sci. 2001;237(1):40-6.
Bolduc C, Shapiro J. Hair care products: waving, straightening, conditioning, and coloring. Clin Dermatol. 2001;19(4):431-6.
Wiesche ESZ, Körner A, Schäfer K, Wortmann FJ. Prevention of hair surface aging. J Cosmet Sci. 2011;62(2):237-49.
de Jager TL, Cockrell AE, Du Plessis SS. Ultraviolet light induced generation of reactive oxygen species. Adv Exp Med Biol. 2017;996:15-23.
Sebetić K, Sjerobabski Masnec I, Cavka V, Biljan D, Krolo I. UV damage of the hair. Coll Antropol. 2008;32(Suppl 2):163-5.
Braida D, Dubief C, Lang G. Photoageing of hair fiber and photoprotection. Skin Pharmacol Physiol. 1994;7(1-2):73-7.
Negre-Salvayre A, Coatrieux C, Ingueneau C, Salvayre R. Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors. Br J Pharmacol. 2008;153(1):6-20.
Iwai I, Hirao T. Protein carbonyls damage the water-holding capacity of the stratum corneum. Skin Pharmacol Physiol. 2008;21(5):269-73.
Slavík J. Anilinonaphthalene sulfonate as a probe of membrane composition and function. Biochim Biophys Acta. 1982;694(1):1-25.
Dennis KJ, Shibamoto T. Gas chromatographic analysis of reactive carbonyl compounds formed from lipids upon UV-irradiation. Lipids. 1990;25(8):460-4.
Hirao T, Takahashi M. Carbonylation of cornified envelopes in the stratum corneum. FEBS Lett. 2005;579(30):6870-4.
Fujita H, Hirao T, Takahashi M. A simple and non-invasive visualization for assessment of carbonylated protein in the stratum corneum. Skin Res Technol. 2007;13(1):84-90.
Fischer MJE. Amine coupling through EDC/NHS: a practical approach. Methods Mol Biol. 2010;627:55-73.
Taneda A, Ogawa H, Hashimoto K. The histochemical demonstration of protein-bound sulfhydryl groups and disulfide bonds in human hair by a new staining method (DACM staining). J Invest Dermatol. 1980;75(4):365-9.
Akagawa M, Suyama K. Oxidative deamination by hydrogen peroxide in the presence of metals. Free Radic Res. 2002;36(1):13-21.
Contributed Indexing:: Keywords: H2O2; acrolein; carbonylation; hair; hydrophobicity
Local Abstract: [Publisher, French] OBJECTIF: l’objectif de cette étude était de clarifier l’impact de la carbonylation des protéines sur les caractéristiques chimiques de la surface des cheveux en se concentrant sur l’hydrophobicité. MÉTHODES: nous avons d’abord examiné la validité de la méthode d’évaluation de l’hydrophobicité, une méthode qui utilise la fluorescence de l’acide 1-anilinonaphtalène-8-sulfonique (1,8-ANS) par rapport aux angles de contact avec l’H2O, de la surface des cheveux chimiquement modifiés par hydrolyse alcaline ou traités par chlorure d’ammonium stéarylique. Nous avons mesuré la fluorescence provenant du 1,8-ANS, l’angle de contact et les modifications des groupes fonctionnels, aldéhydes (le degré de carbonylation), NH2, COOH et SH des cheveux décolorés à l’H2O2 ou traités par acroléine, à l’aide de méthodes de marquage par fluorescence. RÉSULTATS: l’intensité de la fluorescence du 1,8-ANS de la surface des cheveux modifiés chimiquement était bien corrélée aux angles de contact avec l’H2O. Les résultats ont indiqué que le 1,8-ANS était adapté à l’évaluation de l’hydrophobicité de la surface des cheveux. L’hydrophobicité des cheveux décolorés à l’H2O2 ou carbonylés à l’acroléine a diminué. De plus, les modifications des groupes fonctionnels des cheveux carbonylés par l’acroléine ont augmenté, tout comme celles des cheveux décolorés à l’H2O2. CONCLUSION: les résultats suggèrent que la carbonylation des protéines à la surface des cheveux par des aldéhydes diminue l’hydrophobicité et favorise d’autres dommages, tout comme la décoloration.
Substance Nomenclature:: 0 (Aldehydes)
BBX060AN9V (Hydrogen Peroxide)
Entry Date(s):: Date Created: 20211019 Date Completed: 20220131 Latest Revision: 20220131
Update Code:: 20240104
DOI:: 10.1111/ics.12743
PMID:: 34664283
: Czasopismo naukowe

Pełny tekst

Objective: The purpose of this study was to clarify the impact of protein carbonylation on the chemical characteristics of the hair surface focusing on hydrophobicity.
Methods: First, we examined the validity of methods to evaluate hydrophobicity, one that utilizes the fluorescence of 1-anilinonaphtalene-8-sulfonic acid (1,8-ANS) compared with the contact angles against H 2 O, of the hair surface chemically modified by alkaline hydrolysis or treated with stearyl ammonium chloride. We measured hairs bleached with H 2 O 2 or treated with acrolein for fluorescence originating from 1,8-ANS, for the contact angle and for changes of functional groups, aldehydes (the degree of carbonylation), NH 2 , COOH and SH, using fluorescence labelling methods.
Results: The fluorescence intensity of 1,8-ANS of the hair surface modified chemically correlated well with the contact angles against H 2 O. The results indicated that 1,8-ANS is suitable for evaluating the hydrophobicity of the hair surface. The hydrophobicity of hairs bleached with H 2 O 2 or carbonylated with acrolein was decreased. In addition, changes of functional groups in hairs carbonylated with acrolein increased as did those of hairs bleached with H 2 O 2 .
Conclusion: The results suggest that the carbonylation of proteins at the hair surface with aldehydes decreases hydrophobicity and promotes further damage as does bleaching.
(© 2021 Society of Cosmetic Scientists and Societe Francaise de Cosmetologie.)

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