Synthetic scan of C-domain from prion proteins

0370639 - ÚOCHB 2012 CZ eng C - Conference Paper (international conference)
Šebestík, Jaroslav - Zawada, Zbigniew - Šafařík, Martin - Hlaváček, Jan
Synthetic scan of C-domain from prion proteins.
Biologically Active Peptides. 12th Conference. Praha: Institute of Organic Chemistry and Biochemistry AS CR, v. v. i, 2011 - (Slaninová, J.), s. 148-150. Collection Symposium Series, 13. ISBN 978-80-86241-44-9.
[Biologically Active Peptides /12./. Praha (CZ), 27.04.2011-29.04.2011]
R&D Projects: GA ČR GA203/07/1517
Institutional research plan: CEZ:AV0Z40550506
Keywords : prion * peptide thioesters * peptide synthesis * chemical ligation
Subject RIV: CC - Organic Chemistry

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.
Permanent Link: http://hdl.handle.net/11104/0204374