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Affinity-based target deconvolution of safranal

BACKGROUND AND THE PURPOSE OF THE STUDY: 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 hypo...

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Detalles Bibliográficos
Autores principales: Hosseinzadeh, Hossein, Mehri, Soghra, Abolhassani, Mohammad Mahdi, Ramezani, Mohammad, Sahebkar, Amirhossein, Abnous, Khalil
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3614472/
https://www.ncbi.nlm.nih.gov/pubmed/23514587
http://dx.doi.org/10.1186/2008-2231-21-25
Descripción
Sumario:BACKGROUND AND THE PURPOSE OF THE STUDY: 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. RESULTS AND MAJOR CONCLUSION: 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.