Antibiotic properties of novel synthetic temporin A analogs and a cecropin A-temporin a hybrid peptide

Malcolm Richardson, David Wade, Jan Ingmar Flock, Charlotta Edlund, Ingegerd Löfving-Arvholm, Matti Sällberg, Tomas Bergman, Angela Silveira, Cecille Unson, Louise Rollins-Smith, Jerzy Silberring, Malcom Richardson, Pentti Kuusela, Hilkka Lankinen

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Temporin A, 18 analogs, and a cecropin A-temporin A hybrid peptide were tested with antibiotic sensitive and resistant bacteria, fungi, human erythrocytes, and in clotting assays. Several peptides were active in these assays, and some analogs (D-TA, W1-TA, and Con-L4,G10) may be useful lead compounds for further antibiotics development. The activity of temporin A was found to be dependent upon several of its structural features, including amino acid composition and sequence, chirality, helicity, and positive charge.
    Original languageEnglish
    Pages (from-to)533-543
    Number of pages10
    JournalProtein and Peptide Letters
    Volume9
    Issue number6
    DOIs
    Publication statusPublished - 2002

    Keywords

    • Antibiotic peptides
    • Antibiotic resistant bacteria
    • Antifungal
    • Cecropin A
    • Hemolysis
    • Human erythrocyte lysis
    • Ranatuerin 6
    • Temporin A
    • VesCP-M

    Fingerprint

    Dive into the research topics of 'Antibiotic properties of novel synthetic temporin A analogs and a cecropin A-temporin a hybrid peptide'. Together they form a unique fingerprint.

    Cite this