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  1. Article ; Online: The Hypopigmentation Mechanism of Tyrosinase Inhibitory Peptides Derived from Food Proteins: An Overview.

    Song, Yuqiong / Chen, Shengjun / Li, Laihao / Zeng, Yaoxun / Hu, Xiao

    Molecules (Basel, Switzerland)

    2022  Volume 27, Issue 9

    Abstract: Skin hyperpigmentation resulting from excessive tyrosinase expression has long been a problem for beauty lovers, which has not yet been completely solved. Although researchers are working on finding effective tyrosinase inhibitors, most of them are ... ...

    Abstract Skin hyperpigmentation resulting from excessive tyrosinase expression has long been a problem for beauty lovers, which has not yet been completely solved. Although researchers are working on finding effective tyrosinase inhibitors, most of them are restricted, due to cell mutation and cytotoxicity. Therefore, functional foods are developing rapidly for their good biocompatibility. Food-derived peptides have been proven to display excellent anti-tyrosinase activity, and the mechanisms involved mainly include inhibition of oxidation, occupation of tyrosinase's bioactive site and regulation of related gene expression. For anti-oxidation, peptides can interrupt the oxidative reactions catalyzed by tyrosinase or activate an enzyme system, including SOD, CAT, and GSH-Px to scavenge free radicals that stimulate tyrosinase. In addition, researchers predict that peptides probably occupy the site of the substrate by chelating with copper ions or combining with surrounding amino acid residues, ultimately inhibiting the catalytic activity of tyrosinase. More importantly, peptides reduce the tyrosinase expression content, primarily through the cAMP/PKA/CREB pathway, with PI3K/AKT/GSK3β, MEK/ERK/MITF and p38 MAPK/CREB/MITF as side pathways. The objective of this overview is to recap three main mechanisms for peptides to inhibit tyrosinase and the emerging bioinformatic technologies used in developing new inhibitors.
    MeSH term(s) Cell Line, Tumor ; Humans ; Hypopigmentation ; Melanins ; Microphthalmia-Associated Transcription Factor/metabolism ; Monophenol Monooxygenase ; Phosphatidylinositol 3-Kinases/metabolism ; Signal Transduction
    Chemical Substances Melanins ; Microphthalmia-Associated Transcription Factor ; Monophenol Monooxygenase (EC 1.14.18.1)
    Language English
    Publishing date 2022-04-22
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules27092710
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 81: Show issues

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  2. Article: Preparation, purification, and identification of novel antioxidant peptides derived from

    Hu, Xiao / Liu, Jing / Li, Jun / Song, Yuqiong / Chen, Shengjun / Zhou, Shaobo / Yang, Xianqing

    Frontiers in nutrition

    2022  Volume 9, Page(s) 971419

    Abstract: Gracilariopsis ... ...

    Abstract Gracilariopsis lemaneiformis
    Language English
    Publishing date 2022-07-22
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2776676-7
    ISSN 2296-861X
    ISSN 2296-861X
    DOI 10.3389/fnut.2022.971419
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  3. Article ; Online: Copper chelating peptides derived from tilapia (Oreochromis niloticus) skin as tyrosinase inhibitor: Biological evaluation, in silico investigation and in vivo effects.

    Song, Yuqiong / Li, Jun / Tian, Han / Xiang, Huan / Chen, Shengjun / Li, Laihao / Hu, Xiao

    Food research international (Ottawa, Ont.)

    2022  Volume 163, Page(s) 112307

    Abstract: Binuclear copper ions at the active site determine the catalysis of tyrosinase (TYR) ...

    Abstract Binuclear copper ions at the active site determine the catalysis of tyrosinase (TYR)
    MeSH term(s) Animals ; Tilapia/metabolism ; Cichlids/metabolism ; Monophenol Monooxygenase ; Copper ; Zebrafish/metabolism ; Peptides/pharmacology ; Peptides/chemistry ; Ions
    Chemical Substances Monophenol Monooxygenase (EC 1.14.18.1) ; Copper (789U1901C5) ; Peptides ; Ions
    Language English
    Publishing date 2022-12-08
    Publishing country Canada
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1111695-x
    ISSN 1873-7145 ; 0963-9969
    ISSN (online) 1873-7145
    ISSN 0963-9969
    DOI 10.1016/j.foodres.2022.112307
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    In stock of ZB MED Bonn / Germany

    Z 2972: Show issues

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  4. Article ; Online: Inhibiting Osteolytic Breast Cancer Bone Metastasis by Bone-Targeted Nanoagent via Remodeling the Bone Tumor Microenvironment Combined with NIR-II Photothermal Therapy.

    Zeng, Yaoxun / Pan, Zhenxing / Yuan, Jiongpeng / Song, Yuqiong / Feng, Zhenzhen / Chen, Zefeng / Ye, Zhaoyi / Li, Yushan / Bao, Ying / Ran, Zhili / Li, Xinyi / Ye, Huiling / Zhang, Kun / Liu, Xujie / He, Yan

    Small (Weinheim an der Bergstrasse, Germany)

    2023  Volume 19, Issue 38, Page(s) e2301003

    Abstract: Bone is one of the prone metastatic sites of patients with advanced breast cancer. The "vicious cycle" between osteoclasts and breast cancer cells plays an essential role in osteolytic bone metastasis from breast cancer. In order to inhibit bone ... ...

    Abstract Bone is one of the prone metastatic sites of patients with advanced breast cancer. The "vicious cycle" between osteoclasts and breast cancer cells plays an essential role in osteolytic bone metastasis from breast cancer. In order to inhibit bone metastasis from breast cancer, NIR-II photoresponsive bone-targeting nanosystems (CuP@PPy-ZOL NPs) are designed and synthesized. CuP@PPy-ZOL NPs can trigger the photothermal-enhanced Fenton response and photodynamic effect to enhance the photothermal treatment (PTT) effect and thus achieve synergistic anti-tumor effect. Meanwhile, they exhibit a photothermal enhanced ability to inhibit osteoclast differentiation and promote osteoblast differentiation, which reshaped the bone microenvironment. CuP@PPy-ZOL NPs effectively inhibited the proliferation of tumor cells and bone resorption in the in vitro 3D bone metastases model of breast cancer. In a mouse model of breast cancer bone metastasis, CuP@PPy-ZOL NPs combined with PTT with NIR-II significantly inhibited the tumor growth of breast cancer bone metastases and osteolysis while promoting bone repair to achieve the reversal of osteolytic breast cancer bone metastases. Furthermore, the potential biological mechanisms of synergistic treatment are identified by conditioned culture experiments and mRNA transcriptome analysis. The design of this nanosystem provides a promising strategy for treating osteolytic bone metastases.
    MeSH term(s) Animals ; Mice ; Photothermal Therapy ; Tumor Microenvironment ; Bone and Bones/pathology ; Bone Neoplasms/therapy ; Bone Neoplasms/pathology ; Osteoclasts ; Osteolysis/therapy ; Osteolysis/pathology ; Cell Line, Tumor
    Language English
    Publishing date 2023-05-21
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2168935-0
    ISSN 1613-6829 ; 1613-6810
    ISSN (online) 1613-6829
    ISSN 1613-6810
    DOI 10.1002/smll.202301003
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  5. Article: Recovery and identification bioactive peptides from protein isolate of Spirulina platensis and their in vitro effectiveness against oxidative stress‐induced erythrocyte hemolysis

    Zeng, Qiao‐Hui / Wang, Jing Jing / Zhang, Ying‐Hui / Song, Yu‐Qiong / Liang, Jing‐Lin / Zhang, Xue‐Wu

    Journal of the science of food and agriculture. 2020 July, v. 100, no. 9

    2020  

    Abstract: BACKGROUND: Spirulina platensis is recognized as one of the most nutritious foods, containing a high protein content of up to 70%. Meanwhile, he interest in using natural protein resources to develop bioactive peptides is steadily increasing. Therefore, ... ...

    Abstract BACKGROUND: Spirulina platensis is recognized as one of the most nutritious foods, containing a high protein content of up to 70%. Meanwhile, he interest in using natural protein resources to develop bioactive peptides is steadily increasing. Therefore, this study released the bioactive peptides from S. platensis by enzymatic hydrolysis using pepsin (1:3000 U g⁻¹), and their amino acid sequences were determined by de novo sequencing. On this basis, the antioxidant activities of synthesized bioactive peptides were comprehensively evaluated by 2,2′‐azinobis‐3‐ethylbenzothiazolin‐6‐sulfonic acid assay, 1,1‐diphenyl‐2‐picryhydrazyl assay, and cell hemolysis assay induced by 2,2′‐azobis‐(2‐amidino‐propane) dihydrochloride (AAPH). RESULTS: The degree of hydrolysis and recovery percentage of pepsin hydrolysis were 172 and 825 g kg–¹ respectively, and FFEFF (P1: m/z 736.4, 8%), EYFDALA (P2: m/z 828.4, relative intensity 18.5%), and VTAPAASVAL (P3: m/z 899.5, relative intensity 17.3%) were purified and identified. P2 possessed an excellent radical scavenging activity compared with P1, P3, and vitamin C, which was contributed to by its high β‐sheet conformation and specific amino acid compositions. Moreover, P2 significantly attenuated AAPH‐induced oxidative hemolysis of erythrocytes and protected the erythrocytes, because it reduced the formation of malondialdehyde and increased the enzyme activities of superoxide dismutase, catalase, and glutathione peroxidase in erythrocytes. CONCLUSION: This study provided insights into the potential antioxidant function of the synthesized peptides originated from the bioactive peptides of S. platensis proteins, which would contribute to the development of natural antioxidant from new protein resources. © 2020 Society of Chemical Industry
    Keywords Arthrospira platensis ; amino acid composition ; amino acid sequences ; antioxidant activity ; antioxidants ; ascorbic acid ; catalase ; enzymatic hydrolysis ; enzyme activity ; erythrocytes ; foods ; glutathione peroxidase ; hemolysis ; hydrolysis ; malondialdehyde ; pepsin ; peptides ; protein content ; protein isolates ; sulfonic acids ; superoxide dismutase
    Language English
    Dates of publication 2020-07
    Size p. 3776-3782.
    Publishing place John Wiley & Sons, Ltd.
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 184116-6
    ISSN 1097-0010 ; 0022-5142
    ISSN (online) 1097-0010
    ISSN 0022-5142
    DOI 10.1002/jsfa.10408
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 1003: Show issues

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  6. Article ; Online: Recovery and identification bioactive peptides from protein isolate of Spirulina platensis and their in vitro effectiveness against oxidative stress-induced erythrocyte hemolysis.

    Zeng, Qiao-Hui / Wang, Jing Jing / Zhang, Ying-Hui / Song, Yu-Qiong / Liang, Jing-Lin / Zhang, Xue-Wu

    Journal of the science of food and agriculture

    2020  Volume 100, Issue 9, Page(s) 3776–3782

    Abstract: Background: Spirulina platensis is recognized as one of the most nutritious foods, containing a high protein content of up to 70%. Meanwhile, he interest in using natural protein resources to develop bioactive peptides is steadily increasing. Therefore, ...

    Abstract Background: Spirulina platensis is recognized as one of the most nutritious foods, containing a high protein content of up to 70%. Meanwhile, he interest in using natural protein resources to develop bioactive peptides is steadily increasing. Therefore, this study released the bioactive peptides from S. platensis by enzymatic hydrolysis using pepsin (1:3000 U g
    Results: The degree of hydrolysis and recovery percentage of pepsin hydrolysis were 172 and 825 g kg
    Conclusion: This study provided insights into the potential antioxidant function of the synthesized peptides originated from the bioactive peptides of S. platensis proteins, which would contribute to the development of natural antioxidant from new protein resources. © 2020 Society of Chemical Industry.
    MeSH term(s) Antioxidants/chemistry ; Antioxidants/pharmacology ; Catalase/metabolism ; Erythrocytes/cytology ; Erythrocytes/drug effects ; Erythrocytes/metabolism ; Glutathione/metabolism ; Glutathione Peroxidase/metabolism ; Hemolysis/drug effects ; Humans ; Lipid Peroxidation/drug effects ; Malondialdehyde/metabolism ; Oxidative Stress/drug effects ; Peptides/chemistry ; Peptides/pharmacology ; Plant Proteins/chemistry ; Plant Proteins/pharmacology ; Reactive Oxygen Species/metabolism ; Spirulina/chemistry ; Superoxide Dismutase/metabolism
    Chemical Substances Antioxidants ; Peptides ; Plant Proteins ; Reactive Oxygen Species ; Malondialdehyde (4Y8F71G49Q) ; Catalase (EC 1.11.1.6) ; Glutathione Peroxidase (EC 1.11.1.9) ; Superoxide Dismutase (EC 1.15.1.1) ; Glutathione (GAN16C9B8O)
    Language English
    Publishing date 2020-04-27
    Publishing country England
    Document type Journal Article
    ZDB-ID 184116-6
    ISSN 1097-0010 ; 0022-5142
    ISSN (online) 1097-0010
    ISSN 0022-5142
    DOI 10.1002/jsfa.10408
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    In stock of ZB MED Cologne/Königswinter

    Zs.B 808: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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