Document Detail


Molecular analysis of elastic properties of the stratum corneum by solid-state 13C-nuclear magnetic resonance spectroscopy.
MedLine Citation:
PMID:  7537776     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 13C-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 not induce 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 findings suggest 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.
Authors:
Y Jokura; S Ishikawa; H Tokuda; G Imokawa
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of investigative dermatology     Volume:  104     ISSN:  0022-202X     ISO Abbreviation:  J. Invest. Dermatol.     Publication Date:  1995 May 
Date Detail:
Created Date:  1995-06-02     Completed Date:  1995-06-02     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0426720     Medline TA:  J Invest Dermatol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  806-12     Citation Subset:  IM    
Affiliation:
Tochigi Research Laboratories, Kao Corporation, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / pharmacology
Carbon Isotopes
Elasticity
Humans
Keratins / chemistry,  metabolism
Lipids / isolation & purification
Magnetic Resonance Spectroscopy
Microscopy, Electron
Protein Conformation
Rheology
Skin / chemistry
Skin Physiological Phenomena*
Water / analysis
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Carbon Isotopes; 0/Lipids; 68238-35-7/Keratins; 7732-18-5/Water

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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