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Szabó Ildikó

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Tárnoki-Zách Júlia
Evaluation of peptide carrier candidates using tissue barrier models

Aug 30 - szerda

15:30 – 17:00

II. Poszterszekció

P56

Evaluation of peptide carrier candidates using tissue barrier models

Júlia Tárnoki-Zách1, Bence Stipsicz2,3, Előd Méhes1, Ildikó Szabó2,4, Kata Horváti4, Bernadett Pályi5, Zoltán Kis5, Szilvia Bősze3,5 András Czirók1

1 Department of Biological Physics, Eötvös Loránd University, Pázmány Péter sétány 1/A, H-1117, Budapest, Hungary

2 ELKH-ELTE Research Group of Peptide Chemistry, Eötvös Loránd Research Network, Eötvös Loránd University, Pázmány Péter sétány 1/A, H-1117, Budapest, Hungary

3 Doctoral School of Biology, Eötvös Loránd University, Pázmány Péter

sétány 1/C, H-1117, Budapest, Hungary

4 MTA-TTK Lendület Peptide-Based Vaccines Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest H-1117, Hungary.

5 National Public Health Center, Albert Flórián út 2-6, Budapest, 1097, Hungary

Targeting peptides represent a promising approach to improve uptake and efficiency of pharmacological compounds. In vitro barrier models are valuable screening tools to evaluate peptide transport, uptake and toxicity. Here we characterize a number of readily available lung and kidney epithelial cell lines in a transwell barrier model. After forming a monolayer and a subsequent maturation phase of cell-type specific duration, the epithelial cells develop tight junctions on the surface of polycarbonate inserts as evidenced by beta-catenin and ZO1 immunolabeling as well as delayed transport of targeting peptides. Daily monitoring of transepithelial electrical resistance (TEER) values reveal a cell line specific, characteristic time course. Thus, the TEER method with this calibration data offers a non-destructive and agent-free procedure to time pharmacological transport measurements, and to evaluate cytotoxicity of the transported agents. To characterize peptide targeting efficiency, a detector cell layer was cultured in the basolateral compartment of the barrier tissue model. Uptake of fluorescein-labelled peptides was evaluated by flow cytometry. We demonstrate that a derivative of the well-known peptide penetratin that also contains the neuropilin-binding sequence from tuftsin, a naturally occurring tetrapeptide produced by enzymatic cleavage from immunoglobulin G, is better able to pass through barrier layers that expresses its receptor, NRP-1.