Efficacy of a fine fiber film applied with a water-based lotion to improve dry skin.

BACKGROUND: Dry skin can trigger eczema that affects >10% of the US population. Dressing films have been developed to improve diseased skin, but there is limited knowledge about their effects, especially for dry skin-related symptoms. We developed an electrospinning method that creates a coating film, called a fine fiber (FF) film, characterized by the production of a transparent, thin, flexible, and adherent membrane on the skin surface. OBJECTIVE: The aim of this pilot study was to examine the effects of the FF film on dry skin. METHODS: Three treatments (lotion only, lotion with the FF film, and lotion with an alternative film) were designed to treat subjects with rough skin on their lower legs. Twenty-four females were enrolled and used either a water-based lotion U or a petrolatum-based lotion P and the FF film for 2 weeks followed by a regression phase for 1 week. Skin hydration and roughness scores were assessed as were the subjects' perceptions of the effects. RESULTS: When the FF film was applied with lotion U, skin hydration was significantly improved even after 1 week, accompanied by a significant improvement of skin roughness and an increase in skin hydration by the end of the regression phase. An evaluation of moisture permeability suggested that the FF film, especially with lotion U, performed as a semipermeable membrane with optimal moisture healing effects on dry skin. CONCLUSION: The FF film together with a water-based lotion is a promising treatment to quickly improve dry skin conditions.

Coffee polyphenols extracted from green coffee beans improve skin properties and microcirculatory function.

Coffee polyphenols (CPPs), including chlorogenic acid, exert various physiological activities. The purpose of this study was to investigate the effects of CPPs on skin properties and microcirculatory function in humans. In this double-blind, placebo-controlled study, 49 female subjects with mildly xerotic skin received either a test beverage containing CPPs (270 mg/100 mL/day) or a placebo beverage for 8 weeks. The ingestion of CPPs significantly lowered the clinical scores for skin dryness, decreased transepidermal water loss, skin surface pH, and increased stratum corneum hydration and the responsiveness of skin blood flow during local warming. Moreover, the amounts of free fatty acids and lactic acid in the stratum corneum significantly increased after the ingestion of CPPs. These results suggest that an 8-week intake of CPPs improve skin permeability barrier function and hydration, with a concomitant improvement in microcirculatory function, leading to efficacy in the alleviation of mildly xerotic skin.

Homogeneous human complex-type oligosaccharides in correctly folded intact glycoproteins: evaluation of oligosaccharide influence on protein folding, stability, and conformational properties.

The N-glycosylation of proteins is generated at the consensus sequence NXS/T (where X is any amino acid except proline) by the biosynthetic process, and occurs in the endoplasmic reticulum and Golgi apparatus. In order to investigate the influence of human complex-type oligosaccharides on counterpart protein conformation, crambin and ovomucoide, which consist of 46 and 56 amino acid residues, respectively, were selected for synthesis of model glycoproteins. These small glycoproteins were intentionally designed to be glycosylated at the α-helix (crambin: 8 position), ß-sheet (crambin: 2 position) and loop position between the antiparallel ß-sheets (ovomucoide: 28 position), and were synthesized by using a peptide-segment coupling strategy. After preparation of these glycosylated polypeptide chains, protein folding experiments were performed under redox conditions by using cysteine-cystine. Although the small glycoproteins bearing intentional glycosylation at the α-helix and ß-sheet exhibited a suitable folding process, glycosylation at the loop position between the antiparallel ß-strands caused multiple products. The conformational differences in the isolated homogeneous glycoproteins compared with non-glycosylated counterparts were evaluated by circular dichroism (CD) and NMR spectroscopy. These analyses suggested that this intentional N-glycosylation did not result in large conformational changes in the purified protein structures, including the case of glycosylation at the loop position between the antiparallel ß-strands. In addition to these experiments, the conformational properties of three glycoproteins were evaluated by CD spectroscopy under different temperatures. The oligosaccharides on the protein surface fluctuated considerably; this was dependent on the increase in the solution temperature and was thought to disrupt the protein tertiary structure. Based on the measurement of the CD spectra, however, the glycoproteins bearing three disulfide bonds did not exhibit any change in their protein tertiary structure. These results suggest that the oligosaccharide conformational fluctuations were not disruptive to protein tertiary structure, and the tertiary structure of glycoproteins might be stabilized by the disulfide bond network.