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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-3A50-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-189E-8
Genre: Journal Article

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2270975.pdf (Publisher version), 2MB
 
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 Creators:
Sadek, M., Author
Berndt, D., Author
Milovanovic, D.1, Author              
Jahn, R.1, Author              
Diederichsen, U., Author
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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Free keywords: β-peptide; Membranes; Protein-protein interactions; SNARE proteins; Transmembrane domains; Vesicles
 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.

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Language(s): eng - English
 Dates: 2016-02-162016-03-15
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/cbic.201500517
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Title: ChemBioChem
Source Genre: Journal
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Pages: - Volume / Issue: 17 (6) Sequence Number: - Start / End Page: 479 - 485 Identifier: -