Identification of Direct Protein Targets of Small Molecules
Author(s) -
Brett Lomenick,
Richard W. Olsen,
Jing Huang
Publication year - 2010
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb100294v
Subject(s) - chemical biology , small molecule , chemical genetics , identification (biology) , proteome , bottleneck , computational biology , drug discovery , systems biology , biology , computer science , nanotechnology , data science , bioinformatics , genetics , materials science , botany , embedded system
Small-molecule target identification is a vital and daunting task for the chemical biology community as well as for researchers interested in applying the power of chemical genetics to impact biology and medicine. To overcome this "target ID" bottleneck, new technologies are being developed that analyze protein-drug interactions, such as drug affinity responsive target stability (DARTS), which aims to discover the direct binding targets (and off targets) of small molecules on a proteome scale without requiring chemical modification of the compound. Here, we review the DARTS method, discuss why it works, and provide new perspectives for future development in this area.
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