Structure and membrane interactions of the homodimeric antibiotic peptide homotarsinin

0301 basic medicine Circular Dichroism Lipid Bilayers Microbial Sensitivity Tests Calorimetry Gram-Positive Bacteria Article Dynamic Light Scattering Protein Structure, Tertiary 03 medical and health sciences Gram-Negative Bacteria Animals Amino Acid Sequence Anura Dimerization Nuclear Magnetic Resonance, Biomolecular Antimicrobial Cationic Peptides
DOI: 10.1038/srep40854 Publication Date: 2017-01-19T14:10:29Z
ABSTRACT
Abstract Antimicrobial peptides (AMPs) from amphibian skin are valuable template structures to find new treatments against bacterial infections. This work describes for the first time structure and membrane interactions of a homodimeric AMP. Homotarsinin, which was found in Phyllomedusa tarsius anurans, consists two identical cystine-linked polypeptide chains each 24 amino acid residues. The high-resolution monomeric dimeric were determined aqueous buffers. dimer exhibits tightly packed coiled coil three-dimensional structure, keeping hydrophobic residues screened environment. An overall cationic surface assures enhanced with negatively charged membranes. extensive set biophysical data allowed us establish structure-function correlations antimicrobial assays Gram -positive -negative bacteria. Although both present considerable activity, is significantly more effective antibacterial assays.
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