• Korean Chemical Engineering Research
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• v.58 no.1
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• pp.29-35
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• 2020

In this study, the skin permeability was measured by adding cell penetrating peptides, arginine oligomers; (tetra-D-arginine (R4) and hexa-D-arginine (R6)) to little skin-permeable anti-wrinkle peptides (GHK, GHK-Cu, and Pal-GHK), and the results were analyzed by the following six cases. First, in cases where only anti-wrinkle peptides were contained, copper ions (Cu₂⁺) and palmitic acid enhanced the transdermal permeability. Second, when arginine oligomers (R4, R6) were added to GHK, arginine oligomers (R4, R6) increased percutaneous permeability, and R4 showed better percutaneous permeability. Third, the addition of R4 and R6 to GHK-Cu resulted in increased percutaneous transmittance, followed by R6 < R4 percutaneous transmittance. Fourth, when R4 and R6 were added to Pal-GHK, the percutaneous permeability increased with results in R6 < R4 order. Fifth, when R4 was added to GHK, GHK-Cu, and Pal-GHK, the transdermal permeability increased in the order of GHK+R4 < GHK-Cu+R4 < Pal-GHK+R4. Finally, the addition of R6 to GHK, GHK-Cu and Pal-GHK also resulted in increased percutaneous transmittance in the order of GHK+R4 < GHK-Cu+R4 < Pal-GHK+R4. This study provides optimal conditions for enhancing skin absorption of anti-wrinkle peptides GHK, GHK-Cu, and Pal-GHK, and propose a wide range of applications in anti-wrinkle functional cosmetics by suggesting ways to maximize their efficacy.

• Journal of Life Science
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• v.15 no.6 s.73
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• pp.961-967
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• 2005

Macrophage migration inhibitory fartor (MIF), known as a cytokine, is a multifunctional protein that is ubiquitously expressed in a variety of cells and tissues; however, enzymatic function of MIF still remains elusive in cells. In this study, we assessed details of the tautomerase activity of MIF. We established rapid purification condition for MIF by using pGEX system and compared the L-dopachrome tautomerase activity of GST-MIF, tMIF, and MIF. The results show that GST (glutathione S-transferase)-epitope tag or N-terminal amino acids flanking the essential $P^{2}$ almost completely abrogated L-dopachrome tautomerase activity of MIF. Subsequently, to determine whether the N-terminal tags have effects on oligomerization of MIF, protein cross-linking products were analyzed on $15\%$ SDS-PACE. The result demonstrates that N-terminal tags are dispensable for the formation of MIF's homooligomers. Thus, the results imply that exposure of If containing hydrophobic pocket in the active site is critical for L-dopachrome tautomerase activity of MIF. In addition, our study suggest that the MIF's tautomerase activity might be influenced by interacting with cellular partners.