β‑Lactoglobulin Peptide Fragments Conjugated with Caffeic Acid Displaying Dual Activities for Tyrosinase Inhibition and Antioxidant Effect
- Authors
- Yang, Jin-Kyoung; Lee, Eunjin; Hwang, In-Jun; Yim, DaBin; Han, Juhee; Lee, Yoon-Sik; Kim, Jong-Ho
- Issue Date
- Apr-2018
- Publisher
- American Chemical Society
- Keywords
- AMINO-ACID; KOJIC ACID; SKIN; MELANOGENESIS; MELANOCYTE; MELANIN; PROTEIN; CELLS; AMIDE; THIOL
- Citation
- Bioconjugate Chemistry, v.29, no.4, pp.1000 - 1005
- Indexed
- SCIE
SCOPUS
- Journal Title
- Bioconjugate Chemistry
- Volume
- 29
- Number
- 4
- Start Page
- 1000
- End Page
- 1005
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/6359
- DOI
- 10.1021/acs.bioconjchem.8b00050
- ISSN
- 1043-1802
- 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 beta-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 mu M). 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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