A Noninvasive Method for Assessing Interior Skin Damage Caused by Chronological Aging and Photoaging Based on Near-Infrared Diffuse Reflection Spectroscopy

This paper reports a noninvasive method for evaluating skin aging based on near-infrared diffuse reflectance (NIR-DR) spectroscopy. Skin aging can be attributed to photoaging and chronological aging. Both types of aging are heavily involved in the skin changes that occur as we get older, for example...

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Veröffentlicht in:Applied spectroscopy 2008-06, Vol.62 (6), p.677-681
Hauptverfasser: Miyamae, Yuta, Yamakawa, Yumika, Kawabata, Marie, Ozaki, Yukihiro
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Sprache:eng
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Zusammenfassung:This paper reports a noninvasive method for evaluating skin aging based on near-infrared diffuse reflectance (NIR-DR) spectroscopy. Skin aging can be attributed to photoaging and chronological aging. Both types of aging are heavily involved in the skin changes that occur as we get older, for example, wrinkles or sagging skin. Our goal is to develop a noninvasive way to assess changes taking place inside the skin for each type of aging by using NIR-DR spectroscopy. Interior skin damages caused by photoaging and chronological aging were studied for an ultraviolet-B (UVB)-irradiated hairless mouse group (24 mice) and a non-irradiated group (29 mice) by using NIR-DR spectroscopy and principal component analysis (PCA). The results suggested the possibility of monitoring the contribution and the quantitative assessment of both types of aging taking place inside the skin by using the 5990–5490 cm−1 and 5000–4480 cm−1 regions of NIR-DR spectra. For the photoaging, structural changes in proteins are most clearly reflected by a shift of the band near 4880 cm−1 due to a combination of amide A and amide II modes. On the other hand, the chronological aging is associated with a change in collagen quantity as is seen in the intensity changes in NIR bands assigned to collagen. NIR-DR spectroscopy and PCA may allow us to noninvasively assess the degree of photoaging and chronological aging as the degeneration of elasticity in collagen protein and the degradation of protein quantity, respectively.
ISSN:0003-7028
1943-3530
DOI:10.1366/000370208784658156