Document Detail


Structural changes of hair after incorporation of the proline analogue L-azetidine-2-carboxylic acid. A model of hair disease by alteration of primary structure.
MedLine Citation:
PMID:  2408388     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In order to correlate biochemical changes of the hair with physical properties we present a model for the examination techniques. L-azetidine was incorporated into the hair keratin complex and the resulting mechanoelastic properties were determined using the ultramicrohardness testing system on scanning electron microscopy. Structure was investigated by X-ray diffraction and incorporation of L-azetidine was detected by thin-layer chromatography. This system could possibly be introduced for examination of hair changes in humans. 8 white mice, 3 weeks of age, were given L-azetidine-2-carboxylic acid in water (0.1 g/100 ml) as only source of fluid over a period of 5 weeks. They had free access to dry mouse cake only. 8 animals of the same strain, who had free access to tap water and mouse cake and were kept under the same conditions, served as controls. After 5 weeks, the animals were sacrificed and hair was obtained for analyses. 2 dimensional thin-layer chromatography of hair hydrolyzed with 6N HCl at 105 degrees C for 12 hours revealed 2 additional spots in the chromatographic pattern in the experimental animals in comparison with the control group. 1 of the spots was identified as L-azetidine-2-carboxylic acid, while the second spot was possibly a degradation product of L-azetidine on acid hydrolysis at a high temperature. Hair of the animals was put into Mark capillaries and subjected to X-ray diffraction, which showed a markedly disordered orientation of keratin. Impression studies using scanning electron microscopy revealed a remarkably reduced elasticity of hair with incorporated L-azetidine. These findings may be explained on the basis of qualitative or quantitative changes in the helical structure of the keratin complex of hair, which is responsible for the elastic properties, whereas the globular matrix is responsible for the firmness of the hair.
Authors:
G Lubec; A Pollak; H Coradello; H Aschinger; A Wagendristl; H Bangert; K Seifert; E Ratzenhofer
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Wiener klinische Wochenschrift     Volume:  97     ISSN:  0043-5325     ISO Abbreviation:  Wien. Klin. Wochenschr.     Publication Date:  1985 Apr 
Date Detail:
Created Date:  1985-07-25     Completed Date:  1985-07-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  21620870R     Medline TA:  Wien Klin Wochenschr     Country:  AUSTRIA    
Other Details:
Languages:  eng     Pagination:  401-3     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Azetidinecarboxylic Acid / pharmacology*
Azetines / pharmacology*
Chromatography, Thin Layer
Hair / drug effects*,  metabolism,  ultrastructure
Hardness
Keratins / metabolism
Mice
Mice, Inbred Strains
Microscopy, Electron, Scanning
X-Ray Diffraction
Chemical
Reg. No./Substance:
0/Azetines; 2517-04-6/Azetidinecarboxylic Acid; 68238-35-7/Keratins

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


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