Evaluation of tyrosinase inhibitory activity and mechanism of Leucrocin I and its modified peptides

Joompang, Anupong; Jangpromma, Nisachon; Choowongkomon, Kiattawee; Payoungkiattikun, Wisarut; Tankrathok, Anupong; Viyoch, Jarupa; Luangpraditkun, Kunlathida; Klaynongsruang, Sompong

doi:10.1016/j.jbiosc.2020.04.002

Cited by 21 publications

(19 citation statements)

References 28 publications

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“…It is worth mentioning the cellular tyrosinase activity was reduced to 41.18%, 32.94%, and 21.64% by TILI‐2, TILI‐1, and leucrocin I, respectively. It should be noted that both of them showed no cytotoxicity on cells HaCaT and B16F1 up to 1400 μM 64 …”

Section: Semi‐synthetic and Synthetic Peptidesmentioning

confidence: 96%

Naturally occurring and synthetic peptides: Efficient tyrosinase inhibitors

Hariri

Saeedi

Akbarzadeh

2021

Journal of Peptide Science

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Tyrosinase is a copper‐containing enzyme involved in the biosynthesis of melanin pigment, which is the most important photo protective agent against skin photo carcinogenesis. Excess production of melanin causes hyperpigmentation leading to undesired browning in human skin, fruits, and vegetable as well as plant‐derived foods. Moreover, the role of tyrosinase in the onset and progression of various diseases such as cancers, Alzheimer's, and Parkinson diseases has been well documented in the literature. In this respect, tyrosinase inhibitors have been in the center of attention particularly as the efficient skin whitening agents. Among a wide range of compounds possessing anti‐tyrosinase activity, peptides both natural and synthetic derivatives have attracted attention due to high potency and safety.

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Section: Semi‐synthetic and Synthetic Peptidesmentioning

confidence: 96%

Naturally occurring and synthetic peptides: Efficient tyrosinase inhibitors

Hariri

Saeedi

Akbarzadeh

2021

Journal of Peptide Science

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“…Many Cys-containing compounds, such as glutathione, inhibited TYR-catalyzed melanin synthesis by acting as a reactant for the thiol conjugation reaction with DOPAquinone as well as acting as an enzyme inhibitor [ 87 , 88 , 89 ]. A number of peptides from synthetic peptide libraries or natural sources exhibited inhibitory effects against TYR activity in vitro, and some showed antimelanogenic effects at the cell level [ 90 , 101 , 102 , 103 , 104 ]. Relatively high TYR inhibitory activities were achieved by hybrid compounds in which certain peptide sequences were conjugated with kojic acid [ 108 , 109 , 110 ], protocatechuic acid [ 111 ], caffeic acid [ 112 , 113 ], para -coumaric acid [ 113 ], or ascorbic acid [ 114 ].…”

Section: Discussionmentioning

confidence: 99%

“…In cells, ECGYF reduces cellular melanin content more effectively than arbutin or glutathione [ 103 ]. CNGVQPK decreases cellular melanin content more effectively than kojic acid [ 104 ]. FSHHLG-NH 2, RFWG-NH 2 , RLWG-NH 2 , FRWG-NH 2, RFW-NH 2 , RFG-NH 2 , RLG-NH 2 , RLW-NH 2 , WG-NH 2 , and G-NH 2 display very potent antimelanogenic activities in cells compared to arbutin [ 124 , 125 ].…”

Section: Discussionmentioning

confidence: 99%

“…Leucrocin I (NGVQPKY) is an antimicrobial peptide originating from crocodile white blood cell extracts [ 107 ]. Joompang et al reported the mushroom TYR inhibitory activity of leucrocin I (IC 50 >200 μM) and its modified peptides, NGVQPKC (IC 50 = 132 μM) and CNGVQPK (IC 50 = 113 μM), were relatively weaker compared with kojic acid (IC 50 = 26 μM) [ 104 ]. Lineweaver–Burk plots indicated that leucrocin I (NGVQPKY) is a mixed type inhibitor, whereas NGVQPKC and CNGVQPK are competitive inhibitors.…”

Section: Artificial Downregulation Of Melanin Synthesismentioning

confidence: 99%

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Up- or Downregulation of Melanin Synthesis Using Amino Acids, Peptides, and Their Analogs

Boo

2020

Biomedicines

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Harmonious synthesis and distribution of melanin in the skin contribute to the expression of beauty and the maintenance of health. When skin pigmentary disorders occur because of internal or external factors or, when there is a need to artificially increase or reduce the pigmentation level of the skin for aesthetic or therapeutic purposes, various pharmacological therapies are applied but the results are not always satisfactory. Studies have been conducted to improve the efficacy and safety of these treatment strategies. In this review, we present the latest studies regarding peptides and related compounds that may be useful in artificially increasing or reducing skin melanin levels. Certain analogs of α-melanocyte stimulating hormone (MSH) and oligopeptides with the sequences derived from the hormone were shown to promote melanin synthesis in cells and in vivo models. Various amino acids, peptides, their analogs, and their hybrid compounds with other chemical moieties were shown to inhibit tyrosinase (TYR) catalytic activity or downregulate TYR gene expression. Certain peptides were shown to inhibit melanosome biogenesis or induce autophagy, leading to decreased pigmentation. In vivo and clinical evidence are available for some compounds, including [Nle4-D-Phe7]-α-MSH, glutathione disulfide, and glycinamide hydrochloride. For many other compounds, additional studies are required to verify their efficacy and safety in vivo and in clinical trials. The accumulating information regarding pro- and antimelanogenic activity of peptides and related compounds will lead to the development of novel drugs for the treatment of skin pigmentary disorders.

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“…Previously, we reported Tyrosinase Inhibitor Leucrocin I-2 (TILI-2), a peptide derivative from Leucrocin I, can inhibit tyrosinase diphenolase activity and could potentially decrease melanin in cells [ 17 ]. This work builds upon these preliminary findings.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of TILI-2 as an Anti-Tyrosinase, Anti-Oxidative Agent and Its Role in Preventing Melanogenesis Using a Proteomics Approach

et al. 2022

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There is a desire to develop new molecules that can combat hyperpigmentation. To this end, the N-terminal cysteine-containing heptapeptide TILI-2 has shown promising preliminary results. In this work, the mechanism by which it works was evaluated using a series of biochemical assays focusing on known biochemical pathways, followed by LC-MS/MS proteomics to discover pathways that have not been considered before. We demonstrate that TILI-2 is a competitive inhibitor of tyrosinase’s monophenolase activity and it could potentially scavenge ABTS and DPPH radicals. It has a very low cytotoxicity up to 1400 µM against human fibroblast NFDH cells and macrophage-like RAW 264.7 cells. Our proteomics study revealed that another putative mechanism by which TILI-2 may reduce melanin production involves the disruption of the TGF-β signaling pathway in mouse B16F1 cells. This result suggests that TILI-2 has potential scope to be used as a depigmenting agent.

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Evaluation of tyrosinase inhibitory activity and mechanism of Leucrocin I and its modified peptides

Cited by 21 publications

References 28 publications

Naturally occurring and synthetic peptides: Efficient tyrosinase inhibitors

Naturally occurring and synthetic peptides: Efficient tyrosinase inhibitors

Up- or Downregulation of Melanin Synthesis Using Amino Acids, Peptides, and Their Analogs

Evaluation of TILI-2 as an Anti-Tyrosinase, Anti-Oxidative Agent and Its Role in Preventing Melanogenesis Using a Proteomics Approach

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