4.3 Article

Amino Acids and Their N-Acetylated Derivatives Maintain the Skin's Barrier Function

期刊

CHEMICAL & PHARMACEUTICAL BULLETIN
卷 69, 期 7, 页码 652-660

出版社

PHARMACEUTICAL SOC JAPAN
DOI: 10.1248/cpb.c21-00152

关键词

stratum corneum; X-ray diffraction; intercellular lipid; amino acid; N-acetyl-L-hydroxyproline

资金

  1. JSPS KAKENHI [20K08699]
  2. Grants-in-Aid for Scientific Research [20K08699] Funding Source: KAKEN

向作者/读者索取更多资源

The study found that V-acetyl-L-hydroxyproline (AHYP) can maintain skin barrier function by preserving the hydrocarbon-chain packing structure of intercellular lipids through electrostatic repulsion. This suggests that AHYP could be used in skincare formulations to help maintain the skin's barrier function.
The hydrocarbon-chain packing structure of intercellular lipids in the stratum corneum (SC) is critical to the skin's barrier function. We previously found that formation of V-shaped ceramide reduces the barrier function of skin. There are few agents, apart from ceramides and fatty acids that can improve the orthorhombic packing (Orth) ratio of the intercellular lipid packing structure. In this study, we investigated agents that directly increase the Orth ratio. We selected an intercellular lipid model consisting of ceramide, cholesterol, and palmitic acid and performed differential scanning calorimetry. We focused on natural moisturizing factor components in the SC, and therefore investigated amino acids and their derivatives. The results of our intercellular lipid model-based study indicate that .V-acetyl-L-hydroxyproline (AHYP), remarkably, maintains the lamellar structure. We verified the effect of AHYP on the lamellar structure and hydrocarbon chain packing structure of intercellular lipids using time-resolved X-ray diffraction measurements of human SC. We also determined the direct physicochemical effects of AHYP on the Orth ratio of the hydrocarbon-chain packing structure. Hence, the results of our human SC study suggest that AHYP preserves skin barrier function by maintaining the hydrocarbon-chain packing structure of intercellular lipids via electrostatic repulsion. These findings will facilitate the development of skincare formulation that can maintain the skin's barrier function.

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