Conjugation of a novel Apaf-1 inhibitor to peptide-based cell-membrane transporters

Autor:	Laura Mondragón, Isabel Marzo, Glòria Sanclimens, Mar Orzáez, María J. Vicent, Angel Messeguer, Enrique Pérez-Payá
Rok vydání:	2007
Předmět:	Programmed cell death Apoptosis Inhibitor Physiology Cell Peptoid Biology Biochemistry Cell membrane Cellular and Molecular Neuroscience chemistry.chemical_compound Endocrinology medicine.anatomical_structure chemistry Biophysics medicine Viability assay Apoptosome Intracellular
Zdroj:	Peptides. 28:958-968
ISSN:	0196-9781
DOI:	10.1016/j.peptides.2007.02.014
Popis:	We have identified a family of peptoids that inhibits in vitro the activity of the apoptosome, a macromolecular complex that activates mitochondrial-dependent apoptosis pathways. The analysis of peptide-based cell compatible delivery systems of the most active peptoid is presented. The active peptoid was then fused to cell penetrating peptides (CPP) as penetratin (PEN-peptoid) and HIV-1 TAT (TAT-peptoid). PEN-peptoid showed greater cell viability and as a consequence better efficiency as an apoptosis inhibitor than the TAT-peptoid. The intracellular trafficking of both inhibitors was studied by flow cytometry and confocal fluorescence microscopy. Finally, the influence of the cargo (peptoid) molecules on the conformational behavior of the CPP in buffers and in membrane mimetic environments was analyzed using circular dichroism (CD) spectroscopy.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::3b45e0d2d4b07ce0f3519f28df25f5df https://doi.org/10.1016/j.peptides.2007.02.014 Zobrazit plný text záznamu Full Text from ScienceDirect