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
AUTHORS (11)
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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