TY - JOUR
T1 - Detection and Characterization of Catechol Quinone-Derived Protein Adducts Using Biomolecular Mass Spectrometry
AU - Chen, Shu Hui
AU - Li, Chun Wei
N1 - Publisher Copyright:
© Copyright © 2019 Chen and Li.
PY - 2019/8/21
Y1 - 2019/8/21
N2 - The catechol quinone (CQ) motif is present in many biologically relevant molecules throughout endogenous metabolic products, foods, drugs, and environmental pollutants. The CQ derivatives may undergo Michael addition, and has been shown to yield covalent bonds with nucleophilic sites of cysteine, lysine, or histidine residue of proteins. The CQ-adducted proteins may exhibit cytotoxicity or biological functions different from their un-adducted forms. Identification, characterization, and quantification of relevant protein targets are essential but challenging goals. Mass spectrometry (MS) is well-suited for the analysis of proteins and protein modifications. Technical development of bottom-up proteomics has greatly advanced the field of biomolecular MS, including protein adductomics. This mini-review focuses on the use of biomolecular MS in (1) structural and functional characterization of CQ adduction on standards of proteins, (2) identification of endogenous adduction targets, and (3) quantification of adducted blood proteins as exposure index. The reactivity and outcome of CQ adduction are discussed with emphases on endogenous species, such as dopamine and catechol estrogens. Limitations and advancements in sample preparation, MS instrumentation, and software to facilitate protein adductomics are also discussed.
AB - The catechol quinone (CQ) motif is present in many biologically relevant molecules throughout endogenous metabolic products, foods, drugs, and environmental pollutants. The CQ derivatives may undergo Michael addition, and has been shown to yield covalent bonds with nucleophilic sites of cysteine, lysine, or histidine residue of proteins. The CQ-adducted proteins may exhibit cytotoxicity or biological functions different from their un-adducted forms. Identification, characterization, and quantification of relevant protein targets are essential but challenging goals. Mass spectrometry (MS) is well-suited for the analysis of proteins and protein modifications. Technical development of bottom-up proteomics has greatly advanced the field of biomolecular MS, including protein adductomics. This mini-review focuses on the use of biomolecular MS in (1) structural and functional characterization of CQ adduction on standards of proteins, (2) identification of endogenous adduction targets, and (3) quantification of adducted blood proteins as exposure index. The reactivity and outcome of CQ adduction are discussed with emphases on endogenous species, such as dopamine and catechol estrogens. Limitations and advancements in sample preparation, MS instrumentation, and software to facilitate protein adductomics are also discussed.
UR - http://www.scopus.com/inward/record.url?scp=85072739768&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85072739768&partnerID=8YFLogxK
U2 - 10.3389/fchem.2019.00571
DO - 10.3389/fchem.2019.00571
M3 - Review article
AN - SCOPUS:85072739768
SN - 2296-2646
VL - 7
JO - Frontiers in Chemistry
JF - Frontiers in Chemistry
M1 - 571
ER -