Synergic Strategies for the Enhanced Self-Assembly of Biomineralization Peptides for the Synthesis of Functional Nanomaterials

Janairo, Jose Isagani B.; Sakaguchi, Tatsuya; Mine, Kenta; Kamada, Rui; Sakaguchi, Kazuyasu

doi:10.2174/0929866525666171214110206

Cited by 10 publications

(6 citation statements)

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“…Each of these diseases is characterized by a specific amyloidogenic protein, but it has been suggested that a common molecular mechanism governs fibril formation across these diverse systems. Amyloids may also play a variety of functional roles in many organisms and have been regarded as potentially useful nanomaterials in recent years [7][8][9] . Therefore, a detailed characterization of the self-assembling mechanism of amyloid fibrils and the resulting morphology is essential for developing therapeutic strategies for amyloidosis and gaining the knowledge needed to create future nanomaterials.…”

Section: Introductionmentioning

confidence: 99%

Characterization of amyloid β fibril formation under microgravity conditions

et al. 2020

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Amyloid fibrils are self-assembled and ordered proteinaceous supramolecules structurally characterized by the cross-β spine. Amyloid formation is known to be related to various diseases typified by neurogenerative disorders and involved in a variety of functional roles. Whereas common mechanisms for amyloid formation have been postulated across diverse systems, the mesoscopic morphology of the fibrils is significantly affected by the type of solution condition in which it grows. Amyloid formation is also thought to share a phenomenological similarity with protein crystallization. Although many studies have demonstrated the effect of gravity on protein crystallization, its effect on amyloid formation has not been reported. In this study, we conducted an experiment at the International Space Station (ISS) to characterize fibril formation of 40-residue amyloid β (Aβ(1–40)) under microgravity conditions. Our comparative analyses revealed that the Aβ(1–40) fibrilization progresses much more slowly on the ISS than on the ground, similarly to protein crystallization. Furthermore, microgravity promoted the formation of distinct morphologies of Aβ(1–40) fibrils. Our findings demonstrate that the ISS provides an ideal experimental environment for detailed investigations of amyloid formation mechanisms by eliminating the conventionally uncontrollable factors derived from gravity.

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Section: Introductionmentioning

confidence: 99%

Characterization of amyloid β fibril formation under microgravity conditions

et al. 2020

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“…This is an important step towards rational peptide design, which remains a challenge for bionanotechnology. 23 The support or frequency of occurrence of the rules is an important factor to be considered when association rules within a given set of transactions are extracted. 24 Support quanties how frequently an itemset appears in the dataset; in this case, how oen a specic amino acid appears in a particular position in the dataset.…”

Section: Resultsmentioning

confidence: 99%

Sequence rules for gold-binding peptides

Janairo

2023

RSC Adv.

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“…It has been shown that material morphology influences a wide array of the functional properties of nanostructures, including optical, electrical, catalytic, and biological, among others [5][6][7][8][9][10][11]. The use of biomolecules, such as biomineralization peptides, for the synthesis of inorganic nanostructures has gained popularity due to their inherent capacity to self-assemble, combined with their ability to chelate a wide variety of different metal ions [12,13]. It has been shown that biomineralization peptides can be used to create a wide range of inorganic nanomaterials with remarkably diverse structures and chemical properties [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Biomineralization through a Symmetry-Controlled Oligomeric Peptide

Sakaguchi,

Nakagawa,

Mine

et al. 2023

Biomimetics

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Biomineralization peptides are versatile tools for generating nanostructures since they can make specific interactions with various inorganic metals, which can lead to the formation of intricate nanostructures. Previously, we examined the influence that multivalency has on inorganic structures formed by p53 tetramer-based biomineralization peptides and noted a connection between the geometry of the peptide and its ability to regulate nanostructure formation. To investigate the role of multivalency in nanostructure formation by biomineralization peptides more thoroughly, silver biomineralization peptides were engineered by linking them to additional self-assembling molecules based on coiled-coil peptides and multistranded DNA oligomers. Under mild reducing conditions at room temperature, these engineered biomineralization peptides self-assembled and formed silver nanostructures. The trimeric forms of the biomineralization peptides were the most efficient in forming a hexagonal disk nanostructure, with both the coiled-coil peptide and DNA-based multimeric forms. Together, the results suggest that the spatial arrangement of biomineralization peptides plays a more important role in regulating nanostructure formation than their valency.

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Synergic Strategies for the Enhanced Self-Assembly of Biomineralization Peptides for the Synthesis of Functional Nanomaterials

Cited by 10 publications

References 0 publications

Characterization of amyloid β fibril formation under microgravity conditions

Characterization of amyloid β fibril formation under microgravity conditions

Sequence rules for gold-binding peptides

Biomineralization through a Symmetry-Controlled Oligomeric Peptide

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