A piece in the puzzle of deciphering the antimicrobial properties of Histatin 5: The role of arginine-phosphoryl group interaction
IDPs are characterized by a lack of stable tertiary structure under physiological conditions in vitro and it has been shown that ~30% of all proteins in eukaryotic organisms belong to this group, and that IDPs are involved in many central biological processes and diseases. This discovery challenges the traditional protein structure paradigm, which states that a specific, well-defined structure is required for the correct function of a protein. Biochemical evidence has since shown that IDPs are functional, and that the lack of folded structure is related to function. The hypothesis is that IDPs adopts a structure upon adsorption to surfaces that gives rise to a function. Hence, understanding how interactions with surfaces or membranes induces secondary structure of IDPs will shed light on how IDPs perform their functions - that is a fundamental biology question. Here we aim to underpin the role of Arginine-phosphoryl group interactions by studying Histatin 5-membrane interactions, where the lipid contains a phosphorylated headgroup, and compare with our own designed variants of Histatin 5, where the number of Arginine as well as their location in the primary sequence of are altered.
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Marie Skepö; ERIKSSON SKOG Amanda; FRAGNETO Giovanna; GERELLI YURI and MICCIULLA Samantha. (2021). A piece in the puzzle of deciphering the antimicrobial properties of Histatin 5: The role of arginine-phosphoryl group interaction. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1036
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