Comparative analysis of click chemistry mediated activity-based protein profiling in cell lysates
Activity-based protein profiling uses chemical probes that covalently attach to active enzyme targets. Probes with conventional tags have disadvantages, such as limited cell permeability or steric hindrance around the reactive group. A tandem labeling strategy with click chemistry is now widely used...
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| Published in | Molecules (Basel, Switzerland) Vol. 18; no. 10; pp. 12599 - 12608 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
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11.10.2013
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| Abstract | Activity-based protein profiling uses chemical probes that covalently attach to active enzyme targets. Probes with conventional tags have disadvantages, such as limited cell permeability or steric hindrance around the reactive group. A tandem labeling strategy with click chemistry is now widely used to study enzyme targets in situ and in vivo. Herein, the probes are reacted in live cells, whereas the ensuing detection by click chemistry takes place in cell lysates. We here make a comparison of the efficiency of the activity-based tandem labeling strategy by using Cu(I)-catalyzed and strain-promoted click chemistry, different ligands and different lysis conditions. |
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| AbstractList | Activity-based protein profiling uses chemical probes that covalently attach to active enzyme targets. Probes with conventional tags have disadvantages, such as limited cell permeability or steric hindrance around the reactive group. A tandem labeling strategy with click chemistry is now widely used to study enzyme targets in situ and in vivo. Herein, the probes are reacted in live cells, whereas the ensuing detection by click chemistry takes place in cell lysates. We here make a comparison of the efficiency of the activity-based tandem labeling strategy by using Cu(I)-catalyzed and strain-promoted click chemistry, different ligands and different lysis conditions. Activity-based protein profiling uses chemical probes that covalently attach to active enzyme targets. Probes with conventional tags have disadvantages, such as limited cell permeability or steric hindrance around the reactive group. A tandem labeling strategy with click chemistry is now widely used to study enzyme targets in situ and in vivo . Herein, the probes are reacted in live cells, whereas the ensuing detection by click chemistry takes place in cell lysates. We here make a comparison of the efficiency of the activity-based tandem labeling strategy by using Cu(I)-catalyzed and strain-promoted click chemistry, different ligands and different lysis conditions. |
| Author | Yang, Xiaomeng Yang, Yinliang Verhelst, Steven H L |
| AuthorAffiliation | Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany; E-Mails: yinliangyang@gmail.com (Y.Y.); xiaomeng@hotmail.de (X.Y.) |
| AuthorAffiliation_xml | – name: Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany; E-Mails: yinliangyang@gmail.com (Y.Y.); xiaomeng@hotmail.de (X.Y.) |
| Author_xml | – sequence: 1 givenname: Yinliang surname: Yang fullname: Yang, Yinliang email: verhelst@wzw.tum.de organization: Lehrstuhl für Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany. verhelst@wzw.tum.de – sequence: 2 givenname: Xiaomeng surname: Yang fullname: Yang, Xiaomeng – sequence: 3 givenname: Steven H L surname: Verhelst fullname: Verhelst, Steven H L |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24126377$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | activity-based probes Alkynes - chemistry Animals Azide Azides - chemistry Biocatalysis cathepsins Cathepsins - chemistry Cell Extracts - chemistry Cell Fractionation Cell Line Chemical bonds Chemistry Click Chemistry Communication Comparative analysis Copper Sulfate - chemistry Efficiency Enzymes Labeling Ligands Mice Permeability proteases protein modification Proteins Staining and Labeling |
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| Title | Comparative analysis of click chemistry mediated activity-based protein profiling in cell lysates |
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