{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["19(2)"],"submitter":["Worch R"],"pubmed_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 helic"],"journal":["International journal of molecular sciences"],"pagination":["E578"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5855800"],"repository":["biostudies-literature"],"pubmed_title":["Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion."],"pmcid":["PMC5855800"],"pubmed_authors":["Dudek A","Szymaniec A","Setny P","Krupa J","Worch R"],"additional_accession":[]},"is_claimable":false,"name":"Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion.","description":"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 helic","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Feb","modification":"2025-04-26T22:12:59.537Z","creation":"2019-03-26T23:23:11Z"},"accession":"S-EPMC5855800","cross_references":{"pubmed":["29443945"],"doi":["10.3390/ijms19020578"]}}