Article

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

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia.
Biochemical and Biophysical Research Communications (impact factor: 2.48). 12/2004; 325(3):1099-105. DOI:10.1016/j.bbrc.2004.10.115 pp.1099-105
Source: PubMed

ABSTRACT 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.

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Keywords

16 amino acid peptaibol
 
amplitude hinge-bending motions
 
C-terminally spin-labelled peptide analogues
 
forms voltage dependent ion channels
 
helix stabilising propensity
 
hinge region
 
Intermolecular
 
intermolecular interactions
 
N-
 
peptaibol
 
planar lipid bilayers
 
Pro residue
 
rigid helical rod
 
significant conformational rearrangement
 
voltage peptaibol activation
 
zervamicin behaves
 
Zervamicin IIB
 

Zakhar O Shenkarev