A New Water-Soluble Analogue of the Fusion Peptide of Influenza Virus Hemagglutinin: Synthesis and Properties |
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| Authors: | P V Dubovskii M N Zhmak G I Maksaev A S Arseniev |
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| Institution: | (1) Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia;(2) Frumkin Institute of Electrochemistry, Russian Academy of Sciences, Moscow, Russia |
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| Abstract: | A water-soluble analogue F32 of the fusion peptide from influenza virus hemagglutinin was synthesized. It consisted of 32 aa residues and retained the ability to interact with lipid membranes; its N-terminal sequence 1–24 coincided with that of the fusion protein from hemagglutinin (strain A/PR/8/34), whereas residues 25–32 (GGGKKKKK) provided its solubility in water. The peptide induced the conductivity fluctuations in planar bilayer lipid membranes characteristic of active fusion peptides. Conditions were found using CD spectroscopy under which the structure of F32 inside detergent micelles, where it can be studied by high-resolution 1H NMR spectroscopy, is close to the structure of the peptide during its interaction with phospholipid liposomes. |
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| Keywords: | hemagglutinin fusion peptides conductivity fluctuations NMR CD spectroscopy |
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