2010
DOI: 10.1016/j.bpj.2010.09.060
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Dynamic Structure of Bombolitin II Bound to Lipid Bilayers as Revealed by Solid-state NMR and Molecular-Dynamics Simulation

Abstract: Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) membranes were determined by solid-state (31)P and (13)C NMR spectroscopy. (31)P NMR spectra showed that BLT2-DPPC membranes were disrupted into small particles below the gel-to-liquid crystalline phase transition temperature (T(c)) and fused to form a magnetically oriented vesicle system where the membran… Show more

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Cited by 17 publications
(27 citation statements)
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References 35 publications
(82 reference statements)
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“…These results suggest that membrane disruption induced by BLT2 is attributable to insertion of BLT molecules into the lipid bilayer (Fig. 8B) [54].…”
Section: Bombolitin IImentioning
confidence: 95%
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“…These results suggest that membrane disruption induced by BLT2 is attributable to insertion of BLT molecules into the lipid bilayer (Fig. 8B) [54].…”
Section: Bombolitin IImentioning
confidence: 95%
“…The result clearly shows that the helical axis of BLT2 is tilted in the equilibrium state at an angle of 51°relative to the membrane normal. Although the tilt angle determined by MD simulation was a slightly larger than that determined from solid-state NMR experiments, the tilting behavior of BLT2 in a DPPC membrane was nevertheless clearly revealed by both NMR analysis [54] and MD simulation [246]. The secondary structure of BLT2 in the membrane bilayer was investigated by analyzing the main-chain torsion angles ϕ and ψ (Fig.…”
Section: Simulation Of Membrane-bound Peptidesmentioning
confidence: 98%
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