NMR paper Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes st

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[NMR paper] Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes st

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

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Amber

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Homology-based:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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Methyl S2

B-factor

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ArShift- Aromatic

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Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

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11-24-2010, 10:03 PM

nmrlearner

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Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes st

Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.

Related Articles Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.

Chem Phys Lipids. 2004 Nov;132(1):65-77

Authors: Grage SL, Afonin S, Grüne M, Ulrich AS

The interaction of the fusogenic polypeptide segment "B18" from the fertilization protein binding with lipid membranes was investigated by solid state 2H and 31P NMR, and by differential scanning calorimetry. B18 is known to adopt different conformations depending on peptide concentration, ionic conditions, pH and lipid environment. Here, the peptide was studied in its beta-stranded amyloid conformation. According to 31P NMR, the lamellar morphology of the DMPC bilayer remains intact in the presence of B18. In going from low (1:90) to high (1:10) peptide/lipid ratios, an increasing effect on several different 2H-labeled lipid segments was observed, reflecting changes in phase behavior and local dynamics. The strongest influence of B18 was detected at the acyl-chains, while no significant effect on the lipid headgroup conformation was observed. This suggests an insertion of B18 in its fibrillar state into the membrane driven by hydrophobic interactions, rather than a peripheral binding mediated by electrostatics.

PMID: 15530449 [PubMed - indexed for MEDLINE]

Source: PubMed

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