Ni/NiO Core/Shell Nanoparticles for Selective Binding and Magnetic Separation of Histidine-Tagged Proteins

Ni/NiO core/shell nanoparticles having high affinity with polyhistidine were synthesized by decomposition of a Ni surfactant complex followed by air oxidation. Ni/NiO nanoparticles showed selective and efficient binding to histidine-tagged proteins and easy separation by using a magnet. These provid...

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Published inJournal of the American Chemical Society Vol. 128; no. 33; pp. 10658 - 10659
Main Authors Lee, In Su, Lee, Nohyun, Park, Jongnam, Kim, Byung Hyo, Yi, Yong-Weon, Kim, Taeuk, Kim, Tae Kook, Lee, In Hwan, Paik, Seung R, Hyeon, Taeghwan
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 23.08.2006
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Abstract Ni/NiO core/shell nanoparticles having high affinity with polyhistidine were synthesized by decomposition of a Ni surfactant complex followed by air oxidation. Ni/NiO nanoparticles showed selective and efficient binding to histidine-tagged proteins and easy separation by using a magnet. These provided a more convenient way to efficient purification of histidine-tagged proteins compared with the conventional Ni−NTA complex-bound resins and microbeads.
AbstractList Ni/NiO core/shell nanoparticles having high affinity with polyhistidine were synthesized by decomposition of a Ni surfactant complex followed by air oxidation. Ni/NiO nanoparticles showed selective and efficient binding to histidine-tagged proteins and easy separation by using a magnet. These provided a more convenient way to efficient purification of histidine-tagged proteins compared with the conventional Ni-NTA complex-bound resins and microbeads.
Ni/NiO core/shell nanoparticles having high affinity with polyhistidine were synthesized by decomposition of a Ni surfactant complex followed by air oxidation. Ni/NiO nanoparticles showed selective and efficient binding to histidine-tagged proteins and easy separation by using a magnet. These provided a more convenient way to efficient purification of histidine-tagged proteins compared with the conventional Ni−NTA complex-bound resins and microbeads.
Author Yi, Yong-Weon
Lee, In Su
Kim, Byung Hyo
Park, Jongnam
Kim, Tae Kook
Lee, Nohyun
Kim, Taeuk
Paik, Seung R
Hyeon, Taeghwan
Lee, In Hwan
Author_xml – sequence: 1
  givenname: In Su
  surname: Lee
  fullname: Lee, In Su
– sequence: 2
  givenname: Nohyun
  surname: Lee
  fullname: Lee, Nohyun
– sequence: 3
  givenname: Jongnam
  surname: Park
  fullname: Park, Jongnam
– sequence: 4
  givenname: Byung Hyo
  surname: Kim
  fullname: Kim, Byung Hyo
– sequence: 5
  givenname: Yong-Weon
  surname: Yi
  fullname: Yi, Yong-Weon
– sequence: 6
  givenname: Taeuk
  surname: Kim
  fullname: Kim, Taeuk
– sequence: 7
  givenname: Tae Kook
  surname: Kim
  fullname: Kim, Tae Kook
– sequence: 8
  givenname: In Hwan
  surname: Lee
  fullname: Lee, In Hwan
– sequence: 9
  givenname: Seung R
  surname: Paik
  fullname: Paik, Seung R
– sequence: 10
  givenname: Taeghwan
  surname: Hyeon
  fullname: Hyeon, Taeghwan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/16910642$$D View this record in MEDLINE/PubMed
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Snippet Ni/NiO core/shell nanoparticles having high affinity with polyhistidine were synthesized by decomposition of a Ni surfactant complex followed by air oxidation....
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SubjectTerms Histidine - chemistry
Magnetics
Metal Nanoparticles - chemistry
Nickel - chemistry
Protein Binding
Proteins - chemistry
Title Ni/NiO Core/Shell Nanoparticles for Selective Binding and Magnetic Separation of Histidine-Tagged Proteins
URI http://dx.doi.org/10.1021/ja063177n
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