title: Affinity-based target deconvolution of safranal.
abstract: OBJECTIVE
  Affinity-based target deconvolution is an emerging method for the identification of interactions between drugs/drug candidates and cellular proteins, and helps to predict potential activities and side effects of a given compound. In the present study, we hypothesized that a part of safranal pharmacological effects, one of the major constituent of Crocus sativus L., relies on its physical interaction with target proteins.
  
  
  METHODS
  Affinity chromatography solid support was prepared by covalent attachment of safranal to agarose beads. After passing tissue lysate through the column, safranal-bound proteins were isolated and separated on SDS-PAGE or two-dimensional gel electrophoresis. Proteins were identified using MALDI-TOF/TOF mass spectrometry and Mascot software.
  
  
  CONCLUSIONS
  Data showed that safranal physically binds to beta actin, cytochrome b-c1 complex sub-unit 1, trifunctional enzyme sub-unit beta and ATP synthase sub-unit alpha and beta. These interactions may explain part of safranal's pharmacological effects. However, phenotypic and/or biological relevance of these interactions remains to be elucidated by future pharmacological studies.
authors.affiliation: Pharmaceutical Research Center, Department of Medicinal Chemistry, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran. abnouskh@mums.ac.ir.
authors.forename: Hossein
authors.initials: H
authors.lastname: Hosseinzadeh
authors.forename: Soghra
authors.initials: S
authors.lastname: Mehri
authors.forename: Mohammad Mahdi
authors.initials: MM
authors.lastname: Abolhassani
authors.forename: Mohammad
authors.initials: M
authors.lastname: Ramezani
authors.forename: Amirhossein
authors.initials: A
authors.lastname: Sahebkar
authors.forename: Khalil
authors.initials: K
authors.lastname: Abnous