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Open AccessArticle

Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion

1
Institute of Physics, Polish Academy of Sciences, Lotników 32/46 Avenue, 02-668 Warsaw, Poland
2
Centre of New Technologies, University of Warsaw, Banacha 2C Street, 02-097 Warsaw, Poland
3
Institute of Biochemistry and Biophysics Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(2), 578; https://doi.org/10.3390/ijms19020578
Received: 13 December 2017 / Revised: 29 January 2018 / Accepted: 6 February 2018 / Published: 14 February 2018
(This article belongs to the Special Issue Membrane Fusion)
Cleavage of hemagglutinin precursor (HA0) by cellular proteases results in the formation of two subunits, HA1 and HA2. The N-terminal fragment of HA2, named a fusion peptide (HAfp), possess a charged, amine N-terminus. It has been shown that the N-terminus of HAfp stabilizes the structure of a helical hairpin observed for a 23-amino acid long peptide (HAfp1-23), whose larger activity than HAfp1-20 has been demonstrated recently. In this paper, we analyze the effect of N-terminal charge on peptide-mediated fusion efficiency and conformation changes at the membrane interface by comparison with the corresponding N-acetylated peptides of 20- and 23-amino acid lengths. We found that higher fusogenic activities of peptides with unmodified amino termini correlates with their ability to form helical hairpin structures oriented perpendicularly to the membrane plane. Molecular dynamics simulations showed that acetylated peptides adopt open and surface-bound conformation more often, which induced less disorder of the phospholipid chains, as compared to species with unmodified amino termini. View Full-Text
Keywords: viral replication; artificial membrane systems; fluorescence lifetime imaging microscopy; molecular dynamics simulation; phospholipids; peptide termini; peptide-lipid interactions viral replication; artificial membrane systems; fluorescence lifetime imaging microscopy; molecular dynamics simulation; phospholipids; peptide termini; peptide-lipid interactions
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MDPI and ACS Style

Worch, R.; Dudek, A.; Krupa, J.; Szymaniec, A.; Setny, P. Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion. Int. J. Mol. Sci. 2018, 19, 578. https://doi.org/10.3390/ijms19020578

AMA Style

Worch R, Dudek A, Krupa J, Szymaniec A, Setny P. Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion. International Journal of Molecular Sciences. 2018; 19(2):578. https://doi.org/10.3390/ijms19020578

Chicago/Turabian Style

Worch, Remigiusz; Dudek, Anita; Krupa, Joanna; Szymaniec, Anna; Setny, Piotr. 2018. "Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion" Int. J. Mol. Sci. 19, no. 2: 578. https://doi.org/10.3390/ijms19020578

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