Biomimetic and aggregation-driven crystallization route for room-temperature material synthesis

Growth of β-Ga2O 3 nanoparticles on peptide assemblies as nanoreactors

Sangyup Lee, Xueyun Gao, Hiroshi Matsui

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

The room-temperature synthesis of β-Ga2O3 nanocrystal was examined by coupling two biomimetic crystallization techniques, enzymatic peptide nanoassembly templating and aggregation-driven crystallization. The catalytic template of peptide assembly nucleated and mineralized primary β-Ga2O3 crystals and then fused them to grow single-crystalline and monodisperse nanoparticles in the cavity of the peptide assembly at room temperature. In this work, the peptide assembly was exploited as a nanoreactor with an enzymatic functionality catalyzing the hydrolysis of gallium precursors. In addition, the characteristic ring structure of peptide assembly is expected to provide an efficient dehydration pathway and crystallization control over the surface tension, which are advantageous for β-Ga2O3 crystal growth. This multifunctional peptide assembly could be applied for syntheses of a variety of nanomaterials that are kinetically difficult to grow at room temperature.

Original languageEnglish
Pages (from-to)2954-2958
Number of pages5
JournalJournal of the American Chemical Society
Volume129
Issue number10
DOIs
Publication statusPublished - 2007 Mar 14

Fingerprint

Nanoreactors
Biomimetics
Crystallization
Nanoparticles
Peptides
Agglomeration
Temperature
Growth
Gallium
Surface Tension
Nanostructures
Dehydration
Crystal growth
Nanostructured materials
Nanocrystals
Surface tension
Hydrolysis
Crystalline materials
Crystals

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

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abstract = "The room-temperature synthesis of β-Ga2O3 nanocrystal was examined by coupling two biomimetic crystallization techniques, enzymatic peptide nanoassembly templating and aggregation-driven crystallization. The catalytic template of peptide assembly nucleated and mineralized primary β-Ga2O3 crystals and then fused them to grow single-crystalline and monodisperse nanoparticles in the cavity of the peptide assembly at room temperature. In this work, the peptide assembly was exploited as a nanoreactor with an enzymatic functionality catalyzing the hydrolysis of gallium precursors. In addition, the characteristic ring structure of peptide assembly is expected to provide an efficient dehydration pathway and crystallization control over the surface tension, which are advantageous for β-Ga2O3 crystal growth. This multifunctional peptide assembly could be applied for syntheses of a variety of nanomaterials that are kinetically difficult to grow at room temperature.",
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