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Distance regulated vesicle fusion and docking mediated by β-peptide nucleic acid SNARE protein analogues.

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Milovanovic,  D.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Sadek, M., Berndt, D., Milovanovic, D., Jahn, R., & Diederichsen, U. (2016). Distance regulated vesicle fusion and docking mediated by β-peptide nucleic acid SNARE protein analogues. ChemBioChem, 17(6), 479-485. doi:10.1002/cbic.201500517.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-3A50-5
Abstract
Artificial SNARE analogues derived from SNARE proteins, which mediate synaptic membrane fusion, are of interest. They mimic the tetrameric α-helix bundle of the SNARE motif with various bio-oligomer recognition units. Interaction between complementary oligomers linked to the respective membrane by lipid or peptide anchors leads to proximity of vesicles and to fusion of lipid bilayers. β-Peptide nucleic acids were introduced as hybrid oligomers with the native SNARE protein transmembrane/linker sequence, in order to evaluate a fusion system that allows distance tuning of approaching membranes. Formation of a four-base pair β-PNA double strand with 20 Å length is sufficient for vesicle membrane fusion. Elongation of the recognition β-PNA duplex in the linker region yielded a 40 Å β-peptide duplex and provided a vesicle–vesicle distance that only supported hemifusion of vesicle membranes.