Skip to content
2000
Volume 13, Issue 6
  • ISSN: 1573-4064
  • E-ISSN: 1875-6638

Abstract

Small molecule drugs obtained from synthetic compounds or natural products show their therapeutic effects by specifically binding to one or a few target proteins and modulating their functions. In contrast, undesirable drug-protein interactions may provoke harmful side effects. Furthermore, drug-protein interactions also play roles in drug activation, transport, metabolism and regulation of drug resistance. Therefore, systematically identifying binding proteins of a drug molecule is critical for understanding the mechanism of action of the drug at molecular level. In this review, we summarize current widely-used experimental approaches for proteome-wide target identification of small molecule drugs, including affinity purification, chemical proteomics and protein thermal stability based methods. The advance of these methods will quicken the pace of target deconvolution of small molecule drugs and hold promise for drug repositioning research. Moreover, these approaches also provide a powerful arsenal for exploring the signaling pathways of small molecule second messengers, signaling lipids and other regulatory metabolites.

Loading

Article metrics loading...

/content/journals/mc/10.2174/1573406413666170518154724
2017-09-01
2025-06-21
Loading full text...

Full text loading...

/content/journals/mc/10.2174/1573406413666170518154724
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test