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Titolo:
MOLECULAR ANALYSIS OF ELASTIC PROPERTIES OF THE STRATUM-CORNEUM BY SOLID-STATE C-13-NUCLEAR MAGNETIC-RESONANCE SPECTROSCOPY
Autore:
JOKURA Y; ISHIKAWA S; TOKUDA H; IMOKAWA G;
Indirizzi:
KAO CORP,INST FUNDAMENTAL RES,TOCHIGI RES LABS,2606 AKABANE HAGA TOCHIGI JAPAN KAO CORP,INST FUNDAMENTAL RES,TOCHIGI RES LABS HAGA TOCHIGI JAPAN
Titolo Testata:
Journal of investigative dermatology
fascicolo: 5, volume: 104, anno: 1995,
pagine: 806 - 812
SICI:
0022-202X(1995)104:5<806:MAOEPO>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
KERATIN INTERMEDIATE FILAMENTS; BOUND-WATER; PROTEIN FILMS; COILED-COIL; II KERATINS; MOUSE; CONFORMATION; HETERODIMER; HYDRATION; LIPIDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
Y. Jokura et al., "MOLECULAR ANALYSIS OF ELASTIC PROPERTIES OF THE STRATUM-CORNEUM BY SOLID-STATE C-13-NUCLEAR MAGNETIC-RESONANCE SPECTROSCOPY", Journal of investigative dermatology, 104(5), 1995, pp. 806-812

Abstract

To elucidate the precise molecular mechanisms underlying stratum corneum (SC) elasticity, we investigated the molecular dynamics of chemical residues within keratin fibers of human plantar SC under various conditions by cross polarization/magic angle spinning C-13-nuclear magnetic resonance. The intensities of nuclear magnetic resonance spectra responsible for amide carbonyl, C-alpha methine, and side-chain aliphatic carbons in the intact SC decreased markedly with increasing water content of up to 30% in dry SC, and then remained constant at greater than 30%. Lipid extraction of intact SC with acetone/ether (1:1) did notinduce any significant change in the nuclear magnetic resonance spectrum, whereas additional treatment with water, which released natural moisturizing factors (mainly amino acids), caused the SC to lose elasticity. The observed decrease in elasticity of the SC recovered after treatment with basic and neutral amino acids, but not after treatment with acidic amino acid. With the latter treatment, movement of amino acid molecules was significantly disturbed, suggesting a strong interaction with keratin fibers. Parallel studies of the complex elastic modulus of a pig SC sheet with a rheovibron also demonstrated that removal of natural moisturizing factor reduced the elasticity of the SC; this effect was also reversed by the application of basic and neutral amino acids, but not by the application of acidic amino acid. These findingssuggest that structural keratin proteins, mainly consisting of 10-nm filaments, acquire their elasticity with the help of hydrated natural moisturizing factor via the reduction of intermolecular forces, probably through nonhelical regions between keratin fibers.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 14:43:42