2010
DOI: 10.1016/j.jcis.2009.11.043
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Control of the morphology and size of magnetite particles with peptides mimicking the Mms6 protein from magnetotactic bacteria

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Cited by 124 publications
(142 citation statements)
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References 31 publications
(42 reference statements)
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“…Magnetite crystals consisting of (1 0 0) and (1 1 1) faces were obtained in the presence of Mms6 protein, while the crystals consisting of mainly the (1 1 1) face were formed in the absence of this protein (17). A similar observation was reported in an investigation using synthetic peptides mimicking the characteristic amino acids of Mms6 protein (18).…”
supporting
confidence: 81%
See 1 more Smart Citation
“…Magnetite crystals consisting of (1 0 0) and (1 1 1) faces were obtained in the presence of Mms6 protein, while the crystals consisting of mainly the (1 1 1) face were formed in the absence of this protein (17). A similar observation was reported in an investigation using synthetic peptides mimicking the characteristic amino acids of Mms6 protein (18).…”
supporting
confidence: 81%
“…These proteins include Mms5, Mms6, Mms7/MamD, and Mms13/MamC (16). Among these proteins, Mms6 possesses a hydrophobic Leucine-Glycine repeat motif at the N terminus and the hydrophilic region of the C terminus, which is thought to interact with magnetite crystal and iron ions (17)(18). The recombinant Mms6 protein has been shown to mediate the formation of uniform magnetite crystals during in vitro chemical synthesis (16).…”
mentioning
confidence: 99%
“…RS-1 (RS-1) is an ideal system to investigate the range of magnetite biomineralization mechanisms used by MB, because it is the only axenically cultured magnetotactic bacterium outside of the α-Proteobacteria and forms crystals that are irregular or bullet-shaped (11)(12)(13). Recently, the genome of RS-1 was sequenced and found to contain a region resembling a highly edited version of the MAI (14,15). Many of the genes in the RS-1 MAI are highly divergent from their homologs in the magnetotactic α-Proteobacteria, and a number of the genes thought to be important for crystal growth and morphology are absent, raising the question of whether RS-1 has evolved a divergent mechanism of magnetite biomineralization.…”
mentioning
confidence: 99%
“…[288] Mms6 is an amphiphilic protein which mainly consists of an N-terminal hydrophobic region responsible for the self-aggregation of the protein, [289] and C-terminal hydrophilic region containing multiples of acidic amino acids which is suggested to act as an iron-binding site. [290] It was suggested by Arakaki that Mms6 protein is a dominant protein and regulates the biomineralization and controls the morphology of uniform magnetosomes by acting as a template to guide the shape and size of the magnetite crystals formed. [291] Surprisingly, the combination of these biomineral-associating proteins and their mimic peptides has enabled the biomimicking of inorganic materials, especially magnetite nanoparticles.…”
Section: Protein Mediated Synthesis Of Magnetite Nanoparticlesmentioning
confidence: 99%
“…[288] Two main synthetic methods have been used to elucidate the function of the Mms6 protein for preparing magnetite crystals and use the function for an effective biomimicry. [290,293] In the first case, the function of Mms6 during the biomineralization of magnetosomes in BTM was elucidated through the analysis of the Mms6 deletion during the coprecipitation of ferrous and ferric ions. It was concluded that highly ordered cuboidal magnetite crystals consisting of (1 0 0) and (1 1 1) crystal faces with sizes ranging from 20 to 30 nm were formed in the presence of Mms6, while smaller and irregular-shaped magnetite crystals consisting of mainly (1 1 1) faces were formed in the absence of the protein.…”
Section: Protein Mediated Synthesis Of Magnetite Nanoparticlesmentioning
confidence: 99%