Document Detail


Comparative thermodynamic and spectroscopic properties of water interaction with human stratum corneum.
MedLine Citation:
PMID:  19622127     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND/PURPOSE: The water content of skin has a significant impact on skin properties; sufficient hydration is necessary to keep the skin supple, flexible, and smooth. To understand more completely the water retention properties of the human skin barrier, physical macroscopic properties must be related to the structural organization of the stratum corneum (SC). Water, lipids, and natural moisturizing factor (NMF) influence the molecular structures that affect the properties of SC, including water sorption and binding enthalpy. In the research reported here, isothermal microcalorimetry was used to study the interaction of water vapor with isolated human SC in intact, delipidized, and water-washed delipidized forms to identify the influences of the principal components of SC on water sorption. The calorimetric data are interpreted in conjunction with spectroscopic results to identify the conformational changes in keratins induced by lipid and NMF removal and to assess the influence of these changes on water binding in SC. METHODS: Isothermal calorimetry was used to measure the integral heat of water vapor sorption on intact, delipidized, and water-washed delipidized human SC at 32 degrees C as a function of relative humidity using back and thigh skin from three donors. Calorimetric measurements were combined with water vapor sorption measurements to determine the differential thermodynamic properties of these systems. Attenuated total reflection-Fourier transform infrared spectroscopy was used to investigate effects of extraction on protein secondary structure. RESULTS: The magnitudes of the differential enthalpy, entropy, and free energy were greatest for intact SC and least for water-washed delipidized SC. Water sorption followed a similar trend. Delipidization led to a significantly reduced binding enthalpy at low water content; water washing the delipidized SC had only a small additional effect on binding enthalpy. Delipidization converts a fraction of keratin alpha-helixes to turns and random coils, while water sorption converts a fraction of keratin alpha-helixes to beta-sheets, turns, and random coils. CONCLUSIONS: The results of this study are consistent with a water sorption model in which keratin-keratin hydrogen bonds are replaced by keratin-water hydrogen bonds. Delipidization reduces the fraction of dry keratin that is in the alpha-helix conformation, suggesting that lipids hold the keratins in a conformation conducive to optimal hydration.
Authors:
Santosh Yadav; R Randall Wickett; Neville G Pinto; Gerald B Kasting; Stephen W Thiel
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Skin research and technology : official journal of International Society for Bioengineering and the Skin (ISBS) [and] International Society for Digital Imaging of Skin (ISDIS) [and] International Society for Skin Imaging (ISSI)     Volume:  15     ISSN:  1600-0846     ISO Abbreviation:  Skin Res Technol     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-07-22     Completed Date:  2009-10-08     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9504453     Medline TA:  Skin Res Technol     Country:  Denmark    
Other Details:
Languages:  eng     Pagination:  172-9     Citation Subset:  IM    
Affiliation:
Department of Chemical & Materials Engineering, University of Cincinnati, Cincinnati, OH 45221-0012, USA.
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MeSH Terms
Descriptor/Qualifier:
Body Water / metabolism*
Computer Simulation
Humans
Models, Biological
Models, Chemical
Skin / chemistry*,  metabolism*
Skin Absorption / physiology*
Spectrum Analysis / methods*
Thermodynamics
Water / chemistry*,  metabolism*
Chemical
Reg. No./Substance:
7732-18-5/Water

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


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