글로벌 연구동향
분자영상 및 방사화학
- 2018년 05월호
[Bioconjug Chem.] β-Lactoglobulin Peptide Fragments Conjugated with Caffeic Acid Displaying Dual Activities for Tyrosinase Inhibition and Antioxidant Effect.한양대 / 양진경, 김종호*
- 출처
- Bioconjug Chem.
- 등재일
- 2018 Apr 18
- 저널이슈번호
- 29(4):1000-1005. doi: 10.1021/acs.bioconjchem.8b00050. Epub 2018 Mar 15.
- 내용
Abstract
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 (IC50 = 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.
Author informationYang JK1, Lee E2, Hwang IJ1, Yim D1, Han J1, Lee YS2, Kim JH1.
1
Department of Chemical Engineering , Hanyang University , Ansan 426-791 , Republic of Korea.
2
School of Chemical and Biological Engineering , Seoul National University , Seoul 151-744 , Republic of Korea.
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