bc8b00050_si_001.pdf (366.76 kB)
β‑Lactoglobulin Peptide Fragments Conjugated with Caffeic Acid Displaying Dual Activities for Tyrosinase Inhibition and Antioxidant Effect
journal contribution
posted on 2018-03-13, 00:00 authored by Jin-Kyoung Yang, Eunjin Lee, In-Jun Hwang, DaBin Yim, Juhee Han, Yoon-Sik Lee, Jong-Ho KimThe
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.