High stability of the hinge region in the membrane-active peptide helix of zervamicin: paramagnetic relaxation enhancement studies

• Published in: Biochemical and biophysical research communications Vol. 325; no. 3; pp. 1099 - 1105
• Main Authors: Shenkarev, Zakhar O., Paramonov, Alexander S., Balashova, Tamara A., Yakimenko, Zoya A., Baru, Michael B., Mustaeva, Leila G., Raap, Jan, Ovchinnikova, Tatyana V., Arseniev, Alexander S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17.12.2004
• Subjects: Antibiotic; Channel-forming peptide; Ion Channels - analysis; Ion Channels - chemistry; Magnetic Resonance Spectroscopy - methods; Magnetics; Membrane Proteins - analysis; Membrane Proteins - chemistry; Methanol - chemistry; NMR; Peptaibol; Peptaibols; Peptides - analysis; Peptides - chemistry; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Solutions; Structure-Activity Relationship; NMR; Antibiotic; Peptaibol; Channel-forming peptide
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2004.10.115

Zervamicin IIB is a 16 amino acid peptaibol that forms voltage dependent ion channels with multilevel conductance states in planar lipid bilayers and vesicular systems. Stability of the hinge region and intermolecular interactions were investigated in the N- and C-terminally spin-labelled peptide analogues. Intermolecular and intramolecular paramagnetic enhancement indicates that zervamicin behaves as a rigid helical rod in methanol solution. There are no high amplitude hinge-bending motions, and the peptaibol is monomeric up to concentration 1.5 mM. Stability of the hinge region illustrates the helix stabilising propensity of the Pro residue in membrane mimic environments and implies absence of significant conformational rearrangement due to voltage peptaibol activation.