Nguyen The Thuong, Eklouh-Molinier Christophe, Sebiskveradze David, Feru Jezabel, Terryn Christine, Manfait Michel, Brassart-Pasco Sylvie, Piot Olivier
MéDIAN Biophotonique et Technologies pour la Santé, CNRS FRE 3481 MEDyC, SFR Cap-Santé, UFR Pharmacie, Université de Reims Champagne-Ardenne, 51 rue Cognacq-Jay, 51096 Reims Cedex, France.
Analyst. 2014 May 21;139(10):2482-8. doi: 10.1039/c3an00353a.
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.
在皮肤自然老化过程中，真皮结构蛋白的改变会导致形态学变化。这些变化可能是由于I型胶原纤维随着年龄增长发生重排和重新定向，而这一点至今尚未得到研究。傅里叶变换红外光谱显微技术似乎是一种研究正常和病理条件下蛋白质结构的有趣方法。结合偏振器，这种振动技术使我们能够通过计算酰胺I带和酰胺II带积分强度的比值来探测皮肤组织切片内胶原的取向。在本研究中，我们使用偏振傅里叶变换红外成像技术来评估皮肤自然老化过程中真皮胶原的分子变化。偏振红外数据的处理表明，在老年皮肤真皮中，I型胶原纤维与皮肤表面平行。我们的方法可能在皮肤病学以及化妆品领域找到创新应用。
