Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues

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    @article{506765b208684980a064ea167fa39b75,
    title = "Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues",
    abstract = "Rana amurensis is important in Chinese medicine as its skin secretions contain abundant bioactive peptides. Here, we have identified the antimicrobial peptide Amurin-2 and three highly-conserved variants, Amurin-2a, Amurin-2b and Amurin-2c through a combination of molecular cloning and MS/MS fragmentation sequencing. Synthetic replicates of these peptides demonstrate potent antimicrobial activity against S. aureus, whilst some have activity against C.albicans and even resistant bacterial MRSA. Furthermore, two Lys-analogues (K4-Amurin-2 and K11-Amurin-2) were designed to improve the bioactive function and the antimicrobial activity of K4-Amurin-2 against E.coli was enhanced distinctly. In addition, the two modified peptides also showed more potent activity against S. aureus, C. albicans and MRSA strains. Meanwhile, these peptides showed inhibitory effect on the cell viability of several cancer cells. As a result, these structural and functional studies of Amurin-2 variants and analogues could provide insights for future antimicrobial peptide design.",
    keywords = "Amphibian skin secretion; Antimicrobial peptide; Cationicity-related peptide design",
    author = "Luyao Zhang and Xiaoling Chen and Ying Zhang and Chengbang Ma and Xinping Xi and Lei Wang and Mei Zhou and James Burrows and Tianbao Chen",
    year = "2018",
    month = "1",
    day = "31",
    doi = "10.1016/j.bbrc.2018.01.124",
    language = "English",
    pages = "1--11",
    journal = "Biochemical and Biophysical Research Communications",
    issn = "0006-291X",
    publisher = "Academic Press",

    }

    RIS

    TY - JOUR

    T1 - Identification of novel Amurin-2 variants from the skin secretion of Rana amurensis, and the design of cationicity-enhanced analogues

    AU - Zhang, Luyao

    AU - Chen, Xiaoling

    AU - Zhang, Ying

    AU - Ma, Chengbang

    AU - Xi, Xinping

    AU - Wang, Lei

    AU - Zhou, Mei

    AU - Burrows, James

    AU - Chen, Tianbao

    PY - 2018/1/31

    Y1 - 2018/1/31

    N2 - Rana amurensis is important in Chinese medicine as its skin secretions contain abundant bioactive peptides. Here, we have identified the antimicrobial peptide Amurin-2 and three highly-conserved variants, Amurin-2a, Amurin-2b and Amurin-2c through a combination of molecular cloning and MS/MS fragmentation sequencing. Synthetic replicates of these peptides demonstrate potent antimicrobial activity against S. aureus, whilst some have activity against C.albicans and even resistant bacterial MRSA. Furthermore, two Lys-analogues (K4-Amurin-2 and K11-Amurin-2) were designed to improve the bioactive function and the antimicrobial activity of K4-Amurin-2 against E.coli was enhanced distinctly. In addition, the two modified peptides also showed more potent activity against S. aureus, C. albicans and MRSA strains. Meanwhile, these peptides showed inhibitory effect on the cell viability of several cancer cells. As a result, these structural and functional studies of Amurin-2 variants and analogues could provide insights for future antimicrobial peptide design.

    AB - Rana amurensis is important in Chinese medicine as its skin secretions contain abundant bioactive peptides. Here, we have identified the antimicrobial peptide Amurin-2 and three highly-conserved variants, Amurin-2a, Amurin-2b and Amurin-2c through a combination of molecular cloning and MS/MS fragmentation sequencing. Synthetic replicates of these peptides demonstrate potent antimicrobial activity against S. aureus, whilst some have activity against C.albicans and even resistant bacterial MRSA. Furthermore, two Lys-analogues (K4-Amurin-2 and K11-Amurin-2) were designed to improve the bioactive function and the antimicrobial activity of K4-Amurin-2 against E.coli was enhanced distinctly. In addition, the two modified peptides also showed more potent activity against S. aureus, C. albicans and MRSA strains. Meanwhile, these peptides showed inhibitory effect on the cell viability of several cancer cells. As a result, these structural and functional studies of Amurin-2 variants and analogues could provide insights for future antimicrobial peptide design.

    KW - Amphibian skin secretion; Antimicrobial peptide; Cationicity-related peptide design

    UR - https://www.ncbi.nlm.nih.gov/pubmed/29366784

    U2 - 10.1016/j.bbrc.2018.01.124

    DO - 10.1016/j.bbrc.2018.01.124

    M3 - Article

    SP - 1

    EP - 11

    JO - Biochemical and Biophysical Research Communications

    T2 - Biochemical and Biophysical Research Communications

    JF - Biochemical and Biophysical Research Communications

    SN - 0006-291X

    ER -

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