4 research outputs found

    Fig 2 -

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    Risk of acute exacerbation of IBD due to ambient temperature change in NHIS cohort for each temperature quartile (a. cold quartile [-19.4°C–4.3°C], b. cool quartile [4.3–13.7], c. warm quartile [13.7–21.3], d. hot quartile [21.3–33.5]). The risk is described via ORs (dot) with 95% CIs (bar) through single lags (0 to 6) and moving averages (0–1 to 0–6). ORs are estimated with adjustment for daily relative humidity, PM10, NO2, SO2, CO and O3, per 1 °C decrease in daily average temperature for a; per 1 °C increase in daily average temperature for b, c and d. *Abbreviations: IBD, inflammatory bowel disease; NHIS, National Health Insurance Service; OR, odds ratio; CI, confidence interval.</p

    Fig 4 -

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    Risk of acute exacerbation of IBD due to ambient temperature change across temperature deciles in two large cohorts (a. NHIS cohort, b. UK Biobank cohort). The risk is described via ORs (dot) with 95% CIs (bar) when assuming no lag effect (lag 0). ORs are estimated with adjustment for daily relative humidity, PM10, NO2, SO2, CO and O3 in a; with no adjustment in b. The ambient temperature changes are considered per 1 °C decrease in daily average temperature for the first two deciles; per 1 °C increase in daily average temperature for the last eight deciles. *Abbreviations: IBD, inflammatory bowel disease; NHIS, National Health Insurance Service; OR, odds ratio; CI, confidence interval.</p

    β‑Lactoglobulin Peptide Fragments Conjugated with Caffeic Acid Displaying Dual Activities for Tyrosinase Inhibition and Antioxidant Effect

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    The regulation of tyrosinase activity and reactive oxygen species is of great importance for the prevention of dermatological disorders in the fields of medicine and cosmetics. Herein, we report a strategy based on solid-phase peptide chemistry for the synthesis of β-lactoglobulin peptide fragment/caffeic acid (CA) conjugates (CA-Peps) with dual activities of tyrosinase inhibition and antioxidation. The purity of the prepared conjugates, CA-MHIR, CA-HIRL, and CA-HIR, significantly increased to 99%, as acetonide-protected CA was employed in solid-phase coupling reactions on Rink amide resins. The tyrosinase inhibitory activities of all CA-Pep derivatives were higher than the activity of kojic acid, and CA-MHIR exhibited the highest tyrosinase inhibition activity (IC<sub>50</sub> = 47.9 μM). Moreover, CA-Pep derivatives displayed significantly enhanced antioxidant activities in the peroxidation of linoleic acid as compared to the pristine peptide fragments. All CA-Pep derivatives showed no cytotoxicity against B16–F1 melanoma cells
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