Oligo(L-lysine)-induced titanium dioxide

Effects of consecutive lysine on precipitation

Sungjun Ahn, Sangwoo Park, Sangyup Lee

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Biomineralization of metal oxide utilizes biomolecular substances, such as peptides and proteins, to induce mineralization of metal precursors in a mild aqueous solution. In this study, we investigated biomineralization of an abiological substance, titanium dioxide (TiO2), by oligo(L-lysine). Specifically, we systemically studied the influence of the number of consecutive lysine on TiO2 precipitation. Oligo(L-lysine) was chosen as a homopeptide lysine source whose lysine quantity was adjusted. When oligo(L-lysine) contains more than three consecutive lysine, it induces notably fast precipitation, while single and dilysine do not readily form TiO 2 precipitates. Precipitation of TiO2 was promoted with the length of oligo(L-lysine). The oligo(L-lysine) was associated with TiO 2 precipitate, which was confirmed by spectroscopic and thermogravitational analyses. The outcomes of this research provide a plausible rationale for explaining precipitation of the Ti precursor that is highly dependent on peptide sequences.

Original languageEnglish
Pages (from-to)100-105
Number of pages6
JournalJournal of Crystal Growth
Volume335
Issue number1
DOIs
Publication statusPublished - 2011 Nov 15

Fingerprint

Biomineralization
lysine
titanium oxides
Titanium dioxide
Peptides
Lysine
Precipitates
Metals
Proteins
Oxides
peptides
lysyllysine
precipitates
titanium dioxide
metal oxides
aqueous solutions
proteins

All Science Journal Classification (ASJC) codes

  • Condensed Matter Physics
  • Inorganic Chemistry
  • Materials Chemistry

Cite this

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abstract = "Biomineralization of metal oxide utilizes biomolecular substances, such as peptides and proteins, to induce mineralization of metal precursors in a mild aqueous solution. In this study, we investigated biomineralization of an abiological substance, titanium dioxide (TiO2), by oligo(L-lysine). Specifically, we systemically studied the influence of the number of consecutive lysine on TiO2 precipitation. Oligo(L-lysine) was chosen as a homopeptide lysine source whose lysine quantity was adjusted. When oligo(L-lysine) contains more than three consecutive lysine, it induces notably fast precipitation, while single and dilysine do not readily form TiO 2 precipitates. Precipitation of TiO2 was promoted with the length of oligo(L-lysine). The oligo(L-lysine) was associated with TiO 2 precipitate, which was confirmed by spectroscopic and thermogravitational analyses. The outcomes of this research provide a plausible rationale for explaining precipitation of the Ti precursor that is highly dependent on peptide sequences.",
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Oligo(L-lysine)-induced titanium dioxide : Effects of consecutive lysine on precipitation. / Ahn, Sungjun; Park, Sangwoo; Lee, Sangyup.

In: Journal of Crystal Growth, Vol. 335, No. 1, 15.11.2011, p. 100-105.

Research output: Contribution to journalArticle

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AU - Ahn, Sungjun

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AB - Biomineralization of metal oxide utilizes biomolecular substances, such as peptides and proteins, to induce mineralization of metal precursors in a mild aqueous solution. In this study, we investigated biomineralization of an abiological substance, titanium dioxide (TiO2), by oligo(L-lysine). Specifically, we systemically studied the influence of the number of consecutive lysine on TiO2 precipitation. Oligo(L-lysine) was chosen as a homopeptide lysine source whose lysine quantity was adjusted. When oligo(L-lysine) contains more than three consecutive lysine, it induces notably fast precipitation, while single and dilysine do not readily form TiO 2 precipitates. Precipitation of TiO2 was promoted with the length of oligo(L-lysine). The oligo(L-lysine) was associated with TiO 2 precipitate, which was confirmed by spectroscopic and thermogravitational analyses. The outcomes of this research provide a plausible rationale for explaining precipitation of the Ti precursor that is highly dependent on peptide sequences.

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