Journal
ANALYST
Volume 139, Issue 10, Pages 2482-2488Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3an00353a
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Funding
- Champagne-Ardenne Region
- INSERM PNR Imagerie
- CNRS PIR Longevite et Vieillissement
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During chronological skin aging, alterations in dermal structural proteins cause morphological modifications. Modifications are probably due to collagen fiber (type I collagen) rearrangement and reorientation with aging that have not been researched until now. FTIR microspectroscopy appears as an interesting method to study protein structure under normal and pathological conditions. Associated with a polarizer, this vibrational technique permits us to probe collagen orientation within skin tissue sections, by computing the ratio of integrated intensities of amide I and amide II bands. In this study, we used the polarized-FTIR imaging to evaluate molecular modifications of dermal collagen during chronological aging. The data processing of polarized infrared data revealed that type I collagen fibers become parallel to the skin surface in aged skin dermis. Our approach could find innovative applications in dermatology as well as in cosmetics.
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