• Journal of the Society of Cosmetic Scientists of Korea
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• v.46 no.1
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• pp.81-88
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• 2020

Diesel particulate matter (DPM) induces inflammatory cytokines in HaCaT and stimulates XRE promoter activity through AhR binding. Thus, it increases CYP gene family expression. In this study, we have elucidated inhibitory effect of LG Herbal Medicine Complex (LG-HMC) on DPM-induced XRE promoter activity and inflammatory cytokine expression. First of all, the XRE promoter activity was overexpressed by DPM treatment and the LG-HMC abrogated the XRE promoter activity. Morus alba bark extract, Scutellaria baicalensis root extract and constituents of LG-HMC, were found to be main effecters against DPM induced XRE promoter activation. We also found that DPM treatment elevated inflammatory cytokines in HaCaT and the treatment of LG-HMC, Morus alba bark extract and Scutellaria baicalensis root extract down-regulated the DPM induced inflammatory cytokine expression. Additionally, Morus alba bark extract and Scutellaria baicalensis root extract were found to act as free radical scavengers. In conclusion, we confirmed skin protective effect of LG-HMC and uncovered two components, Morus alba bark extract and Scutellaria baicalensis root extract, that play major role in protecting epidermal kertinocytes from damage.

• Bulletin of the Korean Chemical Society
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• v.32 no.8
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• pp.2577-2583
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• 2011

We have designed a 20-residue hybrid peptide CA(1-8)-MA(1-12) (CAMA) incorporating residues 1-8 of cecropin A (CA) and residues 1-12 of magainin 2 (MA) with high bacterial cell selectivity. CAMA-P2 is an ${\alpha}$-helical antimicrobial peptide designed from a CAMA hybrid peptide and substitution of Gly-Ile-Gly hinge sequence of CAMA to Pro influences the flexibility at central part of CAMA. Based on structure-activity relationships of CAMA peptides, to investigate the effects of the total positive charges on antimicrobial activity of CAMA-P2, the $Ser^{14}{\rightarrow}$Lys analogue (CAMA-syn1) was synthesized. The role of tryptophan at C-terminal ${\alpha}$-helix on its antimicrobial activity as well as synergistic activity was also investigated using $Ser^{14}{\rightarrow}$Lys/$Phe^{18}{\rightarrow}$Trp analogue (CAMA-syn2). Also, we designed CAMA-syn3 by substitution of $Lys^{16}$ located opposite side of substituted $Lys^{14}$ of CAMA-syn1 with Leu residue, resulting in increase of hydrophobicity and amphipathicity of the peptide. All of CAMA-syn analogues showed good antimicrobial activities similar to those of CAMA and CAMA-P2. The CAMA-syn1 and CAMA-syn2 showed low hemolytic activity and cytotoxicity against human keratinocyte Haca-T cells while CAMA-syn3 showed hemolytic activity and cytotoxicity at its MIC value. We then investigated their abilities to act synergistically in combination with the antimicrobial flavonoids and synthetic compounds screened in our laboratory. The results showed that all peptides exhibited synergistic effects with dihydrobinetin, while only CAMA-syn2 exhibited synergistic effects with YKAs3001 against both S. aureus and MRSA, suggesting that Trp residue at C-terminus of CAMA-syn2 may facilitate the polar antibiotic flavonoids and synthetic compounds to permeabilize the membrane. This study will be useful for the development of new antibiotic peptides with potent antimicrobial and synergistic activity but without cytotoxicity.