Recent advances in activity-based probes (ABPs) and affinity-based probes (AfBPs) for profiling of enzymes

被引：120

作者：

Fang, Haixiao ^{[1
]}

Peng, Bo ^{[2
]}

Ong, Sing Yee ^{[3
]}

Wu, Qiong ^{[1
]}

Li, Lin ^{[1
]}

Yao, Shao Q. ^{[3
]}

机构：

[1] Nanjing Tech Univ NanjingTech, Inst Adv Mat IAM, Key Lab Flexible Elect KLOFE, 30 South Puzhu Rd, Nanjing 211816, Peoples R China

[2] Northwestern Polytech Univ, Frontiers Sci Ctr Flexible Elect, Xian Inst Flexible Elect IFE, Xian Inst Biomed Mat & Engn, 127 West Youyi Rd, Xian 710072, Peoples R China

[3] Natl Univ Singapore, Dept Chem, 4 Sci Dr 2, Singapore 117544, Singapore

来源：

CHEMICAL SCIENCE | 2021年 / 12卷 / 24期

基金：

新加坡国家研究基金会; 中国国家自然科学基金; 国家重点研发计划;

关键词：

PHOTO-CROSS-LINKERS; IN-SITU; MATRIX METALLOPROTEINASES; DEUBIQUITYLATING ENZYMES; IRREVERSIBLE INHIBITOR; SUBSTRATE-SPECIFICITY; FUNCTIONALIZED NAD(+); PROTEOMICS REVEALS; FLUORESCENT-PROBES; PROTEASE ACTIVITY;

D O I：

10.1039/d1sc01359a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Activity-based protein profiling (ABPP) is a technique that uses highly selective active-site targeted chemical probes to label and monitor the state of proteins. ABPP integrates the strengths of both chemical and biological disciplines. By utilizing chemically synthesized or modified bioactive molecules, ABPP is able to reveal complex physiological and pathological enzyme-substrate interactions at molecular and cellular levels. It is also able to provide critical information of the catalytic activity changes of enzymes, annotate new functions of enzymes, discover new substrates of enzymes, and allow real-time monitoring of the cellular location of enzymes. Based on the mechanism of probe-enzyme interaction, two types of probes that have been used in ABPP are activity-based probes (ABPs) and affinity-based probes (AfBPs). This review highlights the recent advances in the use of ABPs and AfBPs, and summarizes their design strategies (based on inhibitors and substrates) and detection approaches.

引用

页码：8288 / 8310

页数：24

共 176 条

[1] N-Alkylated aziridines are easily-prepared, potent, specific and cell-permeable covalent inhibitors of human β-glucocerebrosidase [J].

Adams, B. T. ;

Niccoli, S. ;

Chowdhury, M. A. ;

Esarik, A. N. K. ;

Lees, S. J. ;

Rempel, B. P. ;

Phenix, C. P. .

CHEMICAL COMMUNICATIONS, 2015, 51 (57) :11390-11393

[2] Cathepsin B: Multiple roles in cancer [J].

Aggarwal, Neha ;

Sloane, Bonnie F. .

PROTEOMICS CLINICAL APPLICATIONS, 2014, 8 (5-6) :427-437

[3] Galacto configured N-aminoaziridines: a new type of irreversible inhibitor of β-galactosidases [J].

Alcaide, Anna ;

Trapero, Ana ;

Perez, Yolanda ;

Llebaria, Amadeu .

ORGANIC & BIOMOLECULAR CHEMISTRY, 2015, 13 (20) :5690-5697

[4] Synthetic Fluorogenic Peptides Reveal Dynamic Substrate Specificity of Depalmitoylases [J].

Amara, Neri ;

Foe, Ian T. ;

Onguka, Ouma ;

Garland, Megan ;

Bogyo, Matthew .

CELL CHEMICAL BIOLOGY, 2019, 26 (01) :35-+

[5] Chemical Tools for Selective Activity Profiling of Endogenously Expressed MMP-14 in Multicellular Models [J].

Amara, Neri ;

Tholen, Martina ;

Bogyo, Matthew .

ACS CHEMICAL BIOLOGY, 2018, 13 (09) :2645-2654

[6] Functionalized Cyclophellitols Are Selective Glucocerebrosidase Inhibitors and Induce a Bona Fide Neuropathic Gaucher Model in Zebrafish [J].

Artola, Marta ;

Kuo, Chi-Lin ;

Lelieveld, Lindsey T. ;

Rowland, Rhianna J. ;

van der Marel, Gijsbert A. ;

Codee, Jeroen D. C. ;

Boot, Rolf G. ;

Davies, Gideon J. ;

G Aerts, Johannes M. F. ;

Overkleeft, Herman S. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2019, 141 (10) :4214-4218

[7] Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes [J].

Bachovchin, Daniel A. ;

Brown, Steven J. ;

Rosen, Hugh ;

Cravatt, Benjamin F. .

NATURE BIOTECHNOLOGY, 2009, 27 (04) :387-394

[8] Advances of small molecule targeting of kinases [J].

Berndt, Norbert ;

Karim, Rezaul M. ;

Schonbrunn, Ernst .

CURRENT OPINION IN CHEMICAL BIOLOGY, 2017, 39 :126-132

[9] The Substrate Specificity of Sirtuins [J].

Bheda, Poonam ;

Jing, Hui ;

Wolberger, Cynthia ;

Lin, Hening .

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85, 2016, 85 :405-429

[10] Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases [J].

Bissaro, Bastien ;

Monsan, Pierre ;

Faure, Regis ;

O'Donohue, Michael J. .

BIOCHEMICAL JOURNAL, 2015, 467 :17-35

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