Journal
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
Volume 411, Issue 2, Pages 387-393Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-018-1445-4
Keywords
Histone acetyltransferase; p300; Cucurbit[8]uril; Peptide assembly; Peptide-templated silver nanoparticles; Electrochemical assay
Funding
- National Natural Science Foundation of China [81503463]
- Science and Technology Planning Project of Taicang [TC2018JC04]
- Natural Science Research Projects of Universities in Jiangsu Province [16KJB430037]
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Accumulating findings demonstrate the importance of histone acetyltransferases (HATs) in regulating the acetylation of histones and reveal that their aberrant catalytic activities are involved in the occurrence and progress of numerous diseases. Herein, a feasible electrochemical method is proposed to assay the activity of HAT. The critical elements of the assay method are the hindrance of HAT-catalyzed acetylation against carboxypeptidase Y-catalyzed digestion and cucurbit[8]uril-assisted peptide assembly, which may recruit peptide-templated silver nanoparticles onto the electrode surface, producing significant electrochemical signals. Taking p300 as a model HAT, the assay method is validated to exhibit desirable selectivity, reproducibility, and usability in inhibitor analysis, and allow absolute activity determination in a linear range from 0.1 to 50nM with a detection limit of 0.055nM, which is lower than those of previous reports. Therefore, this work may provide an effective tool for HAT activity assay, which will be of great potential in HAT-related fundamental research, disease diagnosis, and drug development in the future.
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