Effect of head‐to‐tail cyclization on conformation of histatin‐5 |
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Authors: | Emilia Sikorska Elżbieta Kamysz |
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Affiliation: | Faculty of Chemistry, University of Gdańsk, , 80‐308 Gdansk, Poland |
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Abstract: | Histatin‐5 (Hst‐5, DSHAKRHHGYKRKFHEKHHSHRGY) is a member of a histidine‐rich peptide family secreted by major salivary glands, exhibiting high fungicidal activity against Candida albicans. In the present work, we demonstrate the 3D structure of the head‐to‐tail cyclic variant of Hst‐5 in TFE solution determined using NMR spectroscopy and molecular dynamics simulations. The cyclic histatin‐5 reveals a helix‐loop‐helix motif with α‐helices at positions Ala4‐His7 and Lys11‐Ser20. Both helical segments are arranged relative to each other at an angle of ca. 142°. The head‐to‐tail cyclization increases amphipathicity of the peptide, this, however, does not affect its antimicrobial potency. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd. |
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Keywords: | histatin‐5 head‐to‐tail cyclization antimicrobial peptide NMR molecular dynamics simulations |
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