The membrane interactions and structure of the natural antimicrobial peptide trichogin GA IV have been investigated by CD, ATR FTIR and solid‐state NMR spectroscopy. A model emerges in which the peptide preferentially aligns parallel to the membrane surface and forms dimeric and tetrameric assemblies at higher concentrations.
Trichogin GA IV Alignment and Oligomerization in Phospholipid Bilayers
De Zotti M.;Siano A. S.;Peggion C.;Toniolo C.;
2019
Abstract
The membrane interactions and structure of the natural antimicrobial peptide trichogin GA IV have been investigated by CD, ATR FTIR and solid‐state NMR spectroscopy. A model emerges in which the peptide preferentially aligns parallel to the membrane surface and forms dimeric and tetrameric assemblies at higher concentrations.
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Salnikov_et_al-2019-ChemBioChem.pdf
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