Kojic acid–tripeptide amide as a new tyrosinase inhibitor
نویسندگان
چکیده
منابع مشابه
Kojic Acid Peptide: A New Compound with Anti-Tyrosinase Potential
BACKGROUND Kojic acid was used for decades in the cosmetic industry as an antimelanogenic agent. However, there are two major drawbacks of Kojic acid, one is cytotoxicity and second are instability on storage. These limitations led the scientist to synthesize the active Kojic acid peptides. OBJECTIVE In the present study, we synthesize and investigate the effect of five Kojic acid peptides to...
متن کاملCombined kinetic studies and computational analysis on kojic acid analogous as tyrosinase inhibitors.
Tyrosinase is a key enzyme in melanin synthesis and widely distributed in plants and animals tissues. In mammals, this enzyme is related to pigment production, involved in wound healing, primary immune response and it can also contribute to catecholamines synthesis in the brain. Consequently, tyrosinase enzyme represents an attractive and selective target in the field of the medicine, cosmetics...
متن کاملKojic acid-derived tyrosinase inhibitors: synthesis and bioactivity
Tyrosinase is a key enzyme for melanin biosynthesis, catalyzing the oxidation of L-tyrosine to L-dopaquinone. The tyrosinase inhibition is an effective approach to control hyperpigmentation in human skin and enzymatic browning in fruits and vegetables. Kojic acid is a naturally-occurring tyrosinase inhibitor which has been clinically used to treat the hyperpigmentation of skin. However, kojic a...
متن کاملKojic acid-derived tyrosinase inhibitors: synthesis and bioactivity
Introduction Melanin is a dark pigment produced by about 10% of skin cells in the innermost layer of the epidermis (1). This compound is a heteropolymer of indole derivatives and is produced inside melanosomes through a series of oxidative reactions involving the amino acid tyrosine in the presence of the enzyme tyrosinase (Fig. 1). The type and amount of produced melanin in the melanosomes gen...
متن کاملProbing kojic acid binding to tyrosinase enzyme: insights from a model complex and QM/MM calculations.
An unambiguous picture of the interaction between the inhibitor kojic acid and a model of the dicopper active site of tyrosinase is reported. The observed binding mode probed on bacterial enzyme is confirmed and further refined by QM/MM calculations.
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ژورنال
عنوان ژورنال: Biopolymers
سال: 2007
ISSN: 0006-3525,1097-0282
DOI: 10.1002/bip.20670