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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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 Urheber:
Sadek, M., Autor
Berndt, D., Autor
Milovanovic, D.1, Autor           
Jahn, R.1, Autor           
Diederichsen, U., Autor
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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Schlagwörter: β-peptide; Membranes; Protein-protein interactions; SNARE proteins; Transmembrane domains; Vesicles
 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2016-02-162016-03-15
 Publikationsstatus: Erschienen
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1002/cbic.201500517
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Titel: ChemBioChem
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 17 (6) Artikelnummer: - Start- / Endseite: 479 - 485 Identifikator: -