High stability of the hinge region in the membrane-active peptide helix of zervamicin: paramagnetic relaxation enhancement studies.
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.
Shenkarev
Zakhar O
ZO
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow, Russia.
Paramonov
Alexander S
AS
Balashova
Tamara A
TA
Yakimenko
Zoya A
ZA
Baru
Michael B
MB
Mustaeva
Leila G
LG
Raap
Jan
J
Ovchinnikova
Tatyana V
TV
Arseniev
Alexander S
AS
D007473:Ion Channels / Q000032:analysis / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008280:Magnetics; D008565:Membrane Proteins / Q000032:analysis / Q000737:chemistry*; D000432:Methanol / Q000737:chemistry; D054848:Peptaibols; D010455:Peptides / Q000032:analysis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions; D013329:Structure-Activity Relationship
D007473:Ion Channels; D008565:Membrane Proteins; D054848:Peptaibols; D010455:Peptides; D012996:Solutions; C077077:zervamicin IIB; D000432:Methanol