Identification of lysine K18 acetylation on histone H3 peptide using gold nanoparticles' aggregation behaviour

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• 作者：Ning Li ; Laura Sutarlie ; Qiao Jing Lew ; Sheng-Hao Chao ; Xiaodi Su
• 关键词：Peptide ; functionalized gold nanoparticles ; Colorimetric biosensing ; Histone modification ; Lysine acetylation
• 刊名：Amino Acids
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：48
• 期：4
• 页码：1023-1031
• 全文大小：1,239 KB
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• 作者单位：Ning Li (1)
  Laura Sutarlie (1)
  Qiao Jing Lew (2)
  Sheng-Hao Chao (2) (3)
  Xiaodi Su (1)
  
  1. Institute of Materials Research and Engineering, Agency for Science, Technology and Research (A*STAR), 2 Fusionopolis Way, #08-03, Innovis, Singapore, 138634, Singapore
  2. Expression Engineering Group, Bioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), 20 Biopolis Way, #06-01, Centros, Singapore, 138668, Singapore
  3. Department of Microbiology, National University of Singapore, Block MD4, 5 Science Drive 2, Singapore, 117597, Singapore
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Analytical Chemistry
  Biochemical Engineering
  Life Sciences
  Proteomics
  Neurobiology
  
• 出版者：Springer Wien
• ISSN：1438-2199

文摘

Acetylation of histones, the major protein component of eukaryotic chromosomes, contributes to the epigenetic regulation of gene expression and is also involved in cancer development. A recent study revealed the correlation between tumour formation and acetylation level of lysine K18 on histone H3. In this study, we developed two colorimetric in vitro assays using gold nanoparticles (AuNPs) for identification of lysine K18 acetylation on histone H3 peptide. In assay I, citrate ion-capped AuNP without further modification was employed. Simply mixing the K18 peptide with AuNP solution leads to distinct particle aggregation, relative to that by non-acetylated or lysine K14 acetylated control peptides. In assay II, an AuNP–peptide–antibody composite was synthesized and used as both the sensing probe and the transducing element. By mixing the sample peptides with the composite solution followed by PBS screening, different aggregation behaviours were observed between the K18 acetylated target peptide and the control sequences. Both assays are capable of identifying the acetylated peptides, and also differentiating the distinctive acetylation positions that differ merely by a distance of three amino acids.