Next Article in Journal
Benzothiophenone Derivatives Targeting Mutant Forms of Estrogen Receptor-α in Hormone-Resistant Breast Cancers
Next Article in Special Issue
CD9 and CD81 Interactions and Their Structural Modelling in Sperm Prior to Fertilization
Previous Article in Journal
Cytokeratin-8 in Anaplastic Thyroid Carcinoma: More Than a Simple Structural Cytoskeletal Protein
Previous Article in Special Issue
Mitochondrial Dynamics in Basal and Stressful Conditions
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2018, 19(2), 578; https://doi.org/10.3390/ijms19020578

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.
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)
Full-Text   |   PDF [6597 KB, uploaded 14 February 2018]   |  

Abstract

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
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

SciFeed

Share & Cite This Article

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top