Original title: Synthetic scan of C-domain from prion proteins
Authors: Šebestík, Jaroslav ; Zawada, Zbigniew ; Šafařík, Martin ; Hlaváček, Jan
Document type: Papers
Conference/Event: Biologically Active Peptides /12./, Praha (CZ), 2011-04-27 / 2011-04-29
Year: 2011
Language: eng
Abstract: Prions are suspected as culprits of several neuropathogenic diseases. A combination of chemical and recombinant syntheses is a powerful tool for studying prion role in pathogenesis of neurodegenerative diseases. Due to the presence of “difficult” sequences in the prion protein molecule, chemical ligation procedure using peptide thioesters as key building blocks is a method of choice. Therefore, a synthetic scan of peptides constituting the mouse prion protein (MoPrP) C-domain 93-231 was carried out. The synthesis on chlorotritylchloride resin was the most promising for most peptides. Only the octadecapeptide MoPrP195-212 could not be synthesized by automated peptide synthesis even using the β-sheet breaking dipeptides. This difficulty was overcome by manual peptide synthesis with careful monitoring of coupling and Fmoc removal.
Keywords: chemical ligation; peptide synthesis; peptide thioesters; prion
Project no.: CEZ:AV0Z40550506 (CEP), GA203/07/1517 (CEP)
Funding provider: GA ČR
Host item entry: Biologically Active Peptides. 12th Conference, ISBN 978-80-86241-44-9

Institution: Institute of Organic Chemistry and Biochemistry AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0204374

Permalink: http://www.nusl.cz/ntk/nusl-81032


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Research > Institutes ASCR > Institute of Organic Chemistry and Biochemistry
Conference materials > Papers