Nanostructure Fabrication Based on Engineered α-Synuclein View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2008-07-01

AUTHORS

Natsuki Kobayashi, Sungwoong Han, Chikashi Nakamura, Koji Sode

ABSTRACT

The utilization of biomaterials such as proteins or peptides has recently been focused on as an attractive way to construct nanomaterials by “bottom-up” strategy. We focus on α-synuclein as a novel scaffold material for functional nanomaterial fabrication. This protein constructs an amyloid-like nanostructure by self-assembly under mild conditions. In this paper, we demonstrate nanomaterial fabrication by utilizing two peptide fragments of the non-amyloid-β component of Alzheimer’s disease amyloid region, which is the key region for α-synuclein fibrillation. One of these peptide fragments contains the sequence corresponding to residues 66–82 of wild-type α-synuclein, while the other contains the same region from the Val70Thr/Val71Thr mutant, whose character is drastically different. In this paper, we confirmed that these two peptides individually formed different rod-like structures. Moreover, these peptides modify the fibril nanostructure of full-length α-synuclein, and these effects depend on the peptide sequences. Therefore, we propose the combination of amyloid-forming protein, and its partial peptide fragments with some mutations have a potential for novel nanomaterial fabrication. More... »

PAGES

50-55

References to SciGraph publications

  • 2005-04. Amyloids — a functional coat for microorganisms in NATURE REVIEWS MICROBIOLOGY
  • 2003-09-30. Fabrication of novel biomaterials through molecular self-assembly in NATURE BIOTECHNOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s12030-008-9011-3

    DOI

    http://dx.doi.org/10.1007/s12030-008-9011-3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1021266419


    Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
    Incoming Citations Browse incoming citations for this publication using opencitations.net

    JSON-LD is the canonical representation for SciGraph data.

    TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

    [
      {
        "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
        "about": [
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/03", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Chemical Sciences", 
            "type": "DefinedTerm"
          }, 
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0303", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Macromolecular and Materials Chemistry", 
            "type": "DefinedTerm"
          }
        ], 
        "author": [
          {
            "affiliation": {
              "alternateName": "Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan", 
              "id": "http://www.grid.ac/institutes/grid.136594.c", 
              "name": [
                "Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Kobayashi", 
            "givenName": "Natsuki", 
            "id": "sg:person.01267761644.01", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01267761644.01"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, 2-41-6 Aomi, 135-0064, Tokyo, Koto-ku, Japan", 
              "id": "http://www.grid.ac/institutes/grid.208504.b", 
              "name": [
                "Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan", 
                "Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, 2-41-6 Aomi, 135-0064, Tokyo, Koto-ku, Japan"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Han", 
            "givenName": "Sungwoong", 
            "id": "sg:person.0662612716.91", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0662612716.91"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, 2-41-6 Aomi, 135-0064, Tokyo, Koto-ku, Japan", 
              "id": "http://www.grid.ac/institutes/grid.208504.b", 
              "name": [
                "Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan", 
                "Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, 2-41-6 Aomi, 135-0064, Tokyo, Koto-ku, Japan"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Nakamura", 
            "givenName": "Chikashi", 
            "id": "sg:person.01064174433.10", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01064174433.10"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Department of Technology Risk Management, Graduate School of Technology Management, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan", 
              "id": "http://www.grid.ac/institutes/grid.136594.c", 
              "name": [
                "Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan", 
                "Department of Technology Risk Management, Graduate School of Technology Management, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Sode", 
            "givenName": "Koji", 
            "id": "sg:person.0744652322.82", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0744652322.82"
            ], 
            "type": "Person"
          }
        ], 
        "citation": [
          {
            "id": "sg:pub.10.1038/nrmicro1127", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1023730788", 
              "https://doi.org/10.1038/nrmicro1127"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/nbt874", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1025200827", 
              "https://doi.org/10.1038/nbt874"
            ], 
            "type": "CreativeWork"
          }
        ], 
        "datePublished": "2008-07-01", 
        "datePublishedReg": "2008-07-01", 
        "description": "The utilization of biomaterials such as proteins or peptides has recently been focused on as an attractive way to construct nanomaterials by \u201cbottom-up\u201d strategy. We focus on \u03b1-synuclein as a novel scaffold material for functional nanomaterial fabrication. This protein constructs an amyloid-like nanostructure by self-assembly under mild conditions. In this paper, we demonstrate nanomaterial fabrication by utilizing two peptide fragments of the non-amyloid-\u03b2 component of Alzheimer\u2019s disease amyloid region, which is the key region for \u03b1-synuclein fibrillation. One of these peptide fragments contains the sequence corresponding to residues 66\u201382 of wild-type \u03b1-synuclein, while the other contains the same region from the Val70Thr/Val71Thr mutant, whose character is drastically different. In this paper, we confirmed that these two peptides individually formed different rod-like structures. Moreover, these peptides modify the fibril nanostructure of full-length \u03b1-synuclein, and these effects depend on the peptide sequences. Therefore, we propose the combination of amyloid-forming protein, and its partial peptide fragments with some mutations have a potential for novel nanomaterial fabrication.", 
        "genre": "article", 
        "id": "sg:pub.10.1007/s12030-008-9011-3", 
        "inLanguage": "en", 
        "isAccessibleForFree": false, 
        "isPartOf": [
          {
            "id": "sg:journal.1034468", 
            "issn": [
              "1551-1286", 
              "1551-1294"
            ], 
            "name": "NanoBiotechnology", 
            "publisher": "Springer Nature", 
            "type": "Periodical"
          }, 
          {
            "issueNumber": "1-4", 
            "type": "PublicationIssue"
          }, 
          {
            "type": "PublicationVolume", 
            "volumeNumber": "4"
          }
        ], 
        "keywords": [
          "nanomaterial fabrication", 
          "utilization of biomaterials", 
          "amyloid-like nanostructures", 
          "nanostructure fabrication", 
          "fabrication", 
          "fibril nanostructure", 
          "rod-like structures", 
          "scaffold material", 
          "novel scaffold material", 
          "nanostructures", 
          "Engineered \u03b1", 
          "attractive way", 
          "nanomaterials", 
          "mild conditions", 
          "biomaterials", 
          "peptide sequences", 
          "paper", 
          "amyloid region", 
          "utilization", 
          "materials", 
          "peptide fragments", 
          "potential", 
          "structure", 
          "peptides", 
          "synuclein fibrillation", 
          "protein", 
          "fragments", 
          "sequence", 
          "amyloid-forming proteins", 
          "strategies", 
          "combination", 
          "way", 
          "conditions", 
          "up", 
          "region", 
          "components", 
          "effect", 
          "mutants", 
          "same region", 
          "mutations", 
          "character", 
          "synuclein", 
          "key regions", 
          "fibrillation"
        ], 
        "name": "Nanostructure Fabrication Based on Engineered \u03b1-Synuclein", 
        "pagination": "50-55", 
        "productId": [
          {
            "name": "dimensions_id", 
            "type": "PropertyValue", 
            "value": [
              "pub.1021266419"
            ]
          }, 
          {
            "name": "doi", 
            "type": "PropertyValue", 
            "value": [
              "10.1007/s12030-008-9011-3"
            ]
          }
        ], 
        "sameAs": [
          "https://doi.org/10.1007/s12030-008-9011-3", 
          "https://app.dimensions.ai/details/publication/pub.1021266419"
        ], 
        "sdDataset": "articles", 
        "sdDatePublished": "2022-05-20T07:25", 
        "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
        "sdPublisher": {
          "name": "Springer Nature - SN SciGraph project", 
          "type": "Organization"
        }, 
        "sdSource": "s3://com-springernature-scigraph/baseset/20220519/entities/gbq_results/article/article_467.jsonl", 
        "type": "ScholarlyArticle", 
        "url": "https://doi.org/10.1007/s12030-008-9011-3"
      }
    ]
     

    Download the RDF metadata as:  json-ld nt turtle xml License info

    HOW TO GET THIS DATA PROGRAMMATICALLY:

    JSON-LD is a popular format for linked data which is fully compatible with JSON.

    curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1007/s12030-008-9011-3'

    N-Triples is a line-based linked data format ideal for batch operations.

    curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/s12030-008-9011-3'

    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/s12030-008-9011-3'

    RDF/XML is a standard XML format for linked data.

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/s12030-008-9011-3'


     

    This table displays all metadata directly associated to this object as RDF triples.

    137 TRIPLES      22 PREDICATES      71 URIs      61 LITERALS      6 BLANK NODES

    Subject Predicate Object
    1 sg:pub.10.1007/s12030-008-9011-3 schema:about anzsrc-for:03
    2 anzsrc-for:0303
    3 schema:author N63a9f05f25f5428e869eb37fd298525b
    4 schema:citation sg:pub.10.1038/nbt874
    5 sg:pub.10.1038/nrmicro1127
    6 schema:datePublished 2008-07-01
    7 schema:datePublishedReg 2008-07-01
    8 schema:description The utilization of biomaterials such as proteins or peptides has recently been focused on as an attractive way to construct nanomaterials by “bottom-up” strategy. We focus on α-synuclein as a novel scaffold material for functional nanomaterial fabrication. This protein constructs an amyloid-like nanostructure by self-assembly under mild conditions. In this paper, we demonstrate nanomaterial fabrication by utilizing two peptide fragments of the non-amyloid-β component of Alzheimer’s disease amyloid region, which is the key region for α-synuclein fibrillation. One of these peptide fragments contains the sequence corresponding to residues 66–82 of wild-type α-synuclein, while the other contains the same region from the Val70Thr/Val71Thr mutant, whose character is drastically different. In this paper, we confirmed that these two peptides individually formed different rod-like structures. Moreover, these peptides modify the fibril nanostructure of full-length α-synuclein, and these effects depend on the peptide sequences. Therefore, we propose the combination of amyloid-forming protein, and its partial peptide fragments with some mutations have a potential for novel nanomaterial fabrication.
    9 schema:genre article
    10 schema:inLanguage en
    11 schema:isAccessibleForFree false
    12 schema:isPartOf N010169ebef504d75a815ae5423150255
    13 Nd6b914a03049479f8a6868993444223c
    14 sg:journal.1034468
    15 schema:keywords Engineered α
    16 amyloid region
    17 amyloid-forming proteins
    18 amyloid-like nanostructures
    19 attractive way
    20 biomaterials
    21 character
    22 combination
    23 components
    24 conditions
    25 effect
    26 fabrication
    27 fibril nanostructure
    28 fibrillation
    29 fragments
    30 key regions
    31 materials
    32 mild conditions
    33 mutants
    34 mutations
    35 nanomaterial fabrication
    36 nanomaterials
    37 nanostructure fabrication
    38 nanostructures
    39 novel scaffold material
    40 paper
    41 peptide fragments
    42 peptide sequences
    43 peptides
    44 potential
    45 protein
    46 region
    47 rod-like structures
    48 same region
    49 scaffold material
    50 sequence
    51 strategies
    52 structure
    53 synuclein
    54 synuclein fibrillation
    55 up
    56 utilization
    57 utilization of biomaterials
    58 way
    59 schema:name Nanostructure Fabrication Based on Engineered α-Synuclein
    60 schema:pagination 50-55
    61 schema:productId Nc5fd8adee6904c0398db56c61cb11590
    62 Nf043d1dc8505425a9ff87177c3c351b7
    63 schema:sameAs https://app.dimensions.ai/details/publication/pub.1021266419
    64 https://doi.org/10.1007/s12030-008-9011-3
    65 schema:sdDatePublished 2022-05-20T07:25
    66 schema:sdLicense https://scigraph.springernature.com/explorer/license/
    67 schema:sdPublisher N604c72b246c841e4a01380754925539a
    68 schema:url https://doi.org/10.1007/s12030-008-9011-3
    69 sgo:license sg:explorer/license/
    70 sgo:sdDataset articles
    71 rdf:type schema:ScholarlyArticle
    72 N010169ebef504d75a815ae5423150255 schema:volumeNumber 4
    73 rdf:type schema:PublicationVolume
    74 N23cd6999d7ea4c90ad92567fc46f1bf0 rdf:first sg:person.0744652322.82
    75 rdf:rest rdf:nil
    76 N466f64162f2247e7a2f4e5ced90827f4 rdf:first sg:person.01064174433.10
    77 rdf:rest N23cd6999d7ea4c90ad92567fc46f1bf0
    78 N604c72b246c841e4a01380754925539a schema:name Springer Nature - SN SciGraph project
    79 rdf:type schema:Organization
    80 N62462fcb19e74fdd91d72c0010764afc rdf:first sg:person.0662612716.91
    81 rdf:rest N466f64162f2247e7a2f4e5ced90827f4
    82 N63a9f05f25f5428e869eb37fd298525b rdf:first sg:person.01267761644.01
    83 rdf:rest N62462fcb19e74fdd91d72c0010764afc
    84 Nc5fd8adee6904c0398db56c61cb11590 schema:name dimensions_id
    85 schema:value pub.1021266419
    86 rdf:type schema:PropertyValue
    87 Nd6b914a03049479f8a6868993444223c schema:issueNumber 1-4
    88 rdf:type schema:PublicationIssue
    89 Nf043d1dc8505425a9ff87177c3c351b7 schema:name doi
    90 schema:value 10.1007/s12030-008-9011-3
    91 rdf:type schema:PropertyValue
    92 anzsrc-for:03 schema:inDefinedTermSet anzsrc-for:
    93 schema:name Chemical Sciences
    94 rdf:type schema:DefinedTerm
    95 anzsrc-for:0303 schema:inDefinedTermSet anzsrc-for:
    96 schema:name Macromolecular and Materials Chemistry
    97 rdf:type schema:DefinedTerm
    98 sg:journal.1034468 schema:issn 1551-1286
    99 1551-1294
    100 schema:name NanoBiotechnology
    101 schema:publisher Springer Nature
    102 rdf:type schema:Periodical
    103 sg:person.01064174433.10 schema:affiliation grid-institutes:grid.208504.b
    104 schema:familyName Nakamura
    105 schema:givenName Chikashi
    106 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01064174433.10
    107 rdf:type schema:Person
    108 sg:person.01267761644.01 schema:affiliation grid-institutes:grid.136594.c
    109 schema:familyName Kobayashi
    110 schema:givenName Natsuki
    111 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01267761644.01
    112 rdf:type schema:Person
    113 sg:person.0662612716.91 schema:affiliation grid-institutes:grid.208504.b
    114 schema:familyName Han
    115 schema:givenName Sungwoong
    116 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0662612716.91
    117 rdf:type schema:Person
    118 sg:person.0744652322.82 schema:affiliation grid-institutes:grid.136594.c
    119 schema:familyName Sode
    120 schema:givenName Koji
    121 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0744652322.82
    122 rdf:type schema:Person
    123 sg:pub.10.1038/nbt874 schema:sameAs https://app.dimensions.ai/details/publication/pub.1025200827
    124 https://doi.org/10.1038/nbt874
    125 rdf:type schema:CreativeWork
    126 sg:pub.10.1038/nrmicro1127 schema:sameAs https://app.dimensions.ai/details/publication/pub.1023730788
    127 https://doi.org/10.1038/nrmicro1127
    128 rdf:type schema:CreativeWork
    129 grid-institutes:grid.136594.c schema:alternateName Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan
    130 Department of Technology Risk Management, Graduate School of Technology Management, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan
    131 schema:name Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan
    132 Department of Technology Risk Management, Graduate School of Technology Management, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan
    133 rdf:type schema:Organization
    134 grid-institutes:grid.208504.b schema:alternateName Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, 2-41-6 Aomi, 135-0064, Tokyo, Koto-ku, Japan
    135 schema:name Department of Biotechnology, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, 184-8588, Tokyo, Koganei, Japan
    136 Research Institute for Cell Engineering, National Institute of Advanced Industrial Science and Technology, 2-41-6 Aomi, 135-0064, Tokyo, Koto-ku, Japan
    137 rdf:type schema:Organization
     




    Preview window. Press ESC to close (or click here)


    ...