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MALDI‐MS Patterning of Caspase Activities and Its Application in the Assessment of Drug Resistance
Author(s) -
Hu Junjie,
Liu Fei,
Ju Huangxian
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201601096
Subject(s) - chemistry , cleavage (geology) , peptide , enzyme , caspase , apoptosis , nanotechnology , biochemistry , materials science , programmed cell death , fracture (geology) , composite material
Mass spectrometry (MS) has been widely used for enzyme activity assays. Herein, we propose a MALDI‐MS patterning strategy for the convenient visual presentation of multiple enzyme activities with an easy‐to‐prepare chip. The array‐based caspase‐activity patterned chip (Casp‐PC) is fabricated by hydrophobically assembling different phospholipid‐tagged peptide substrates on a modified ITO slide. The advantages of amphipathic phospholipids lead to high‐quality mass spectra for imaging analysis. Upon the respective cleavage of these substrates by different caspases, such as caspase‐1, ‐2, ‐3, and ‐8, to produce a mass shift, the enzyme activities can be directly evaluated by MALDI‐MS patterning by m / z ‐dependent imaging of the cleavage products. The ability to identify drug‐sensitive/resistant cancer cells and assess the curative effects of anticancer drugs is demonstrated, indicating the applicability of the method and the designed chip.