Abstract
The role of magnetosome associated proteins on the in vitro synthesis of magnetite nanoparticles has gained interest, both to obtain a better understanding of the magnetosome biomineralization process and to be able to produce novel magnetosome-like biomimetic nanoparticles. Up to now, only one recombinant protein has been used at the time to in vitro form biomimetic magnetite precipitates, being that a scenario far enough from what probably occurs in the magnetosome. In the present study, both Mms6 and MamC from Magnetococcus marinus MC-1 have been used to in vitro form biomimetic magnetites. Our results show that MamC and Mms6 have different, but complementary, effects on in vitro magnetite nucleation and growth. MamC seems to control the kinetics of magnetite nucleation while Mms6 seems to preferably control the kinetics for crystal growth. Our results from the present study also indicate that it is possible to combine both proteins to tune the properties of the resulting biomimetic magnetites. In particular, by changing the relative ratio of these proteins, better faceted and/or larger magnetite crystals with, consequently, different magnetic moment per particle could be obtained. This study provides with tools to obtain new biomimetic nanoparticles with a potential utility for biotechnological applications.
Highlights
Magnetotactic bacteria form an ubiquitous and heterogeneous group of prokaryotic microorganisms that possess an unique organelle, the magnetosome, formed by a magnetic mineral [magnetite (Fe3O4) or greigite (Fe2S4)] surrounded by a lipid bilayer[1,2,3,4]
The goal of this paper is to determine the effect of introducing two magnetosome associated proteins (MAPs), Mms[6] and MamC from Magnetococcus marinus MC-1, expressed as full length recombinant proteins, at different ratios in the reaction mixture from which magnetite precipitates, being the first time in which two proteins from the same magnetotactic bacteria have been introduced in the same reaction mixture
In the context of the individual effect of each protein on the in vitro magnetite nucleation and growth, Nudelman and Zarivach[15] predicted that the secondary structure of Mms[6] from Magnetospirillum gryphiswaldense MSR-1 shows an unstructured N-terminal with a transmembrane region and an acidic C-terminal, which may form an α-helix structure, which is exposed to the magnetosome lumen and, it would be able to interact with the magnetite crystal
Summary
Magnetotactic bacteria form an ubiquitous and heterogeneous group of prokaryotic microorganisms that possess an unique organelle, the magnetosome, formed by a magnetic mineral [magnetite (Fe3O4) or greigite (Fe2S4)] surrounded by a lipid bilayer[1,2,3,4]. Mms[6], MamD (Mms7), MamC (Mms13), MamG (Mms5) and MmsF are MAPs already identified as candidates to in vitro produce biomimetic magnetic nanoparticles (BMNPs)[15,16,31,32] In this context, much work has been done by using Mms[6] (either full length expressed as recombinant protein or synthetic peptides) from Magnetospirillum magneticum AMB118–22,24,25,27,28. The goal of this paper is to determine the effect of introducing two MAPs, Mms[6] and MamC from Magnetococcus marinus MC-1, expressed as full length recombinant proteins, at different ratios in the reaction mixture from which magnetite precipitates, being the first time in which two proteins from the same magnetotactic bacteria have been introduced in the same reaction mixture. This is the first time that Mms[6] from Magnetococcus marinus MC-1 is expressed as recombinant protein, purified and used to in vitro precipitate magnetite
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