Table of Contents
International Journal of Peptides
Volume 2013 (2013), Article ID 197317, 9 pages
http://dx.doi.org/10.1155/2013/197317
Research Article

Development of the Schedule for Multiple Parallel “Difficult” Peptide Synthesis on Pins

Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, 10 Pogodinskaya Ulica, Moscow 119121, Russia

Received 30 April 2013; Accepted 9 July 2013

Academic Editor: John D. Wade

Copyright © 2013 Ekaterina F. Kolesanova et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Unified schedule for multiple parallel solid-phase synthesis of so-called “difficult” peptides on polypropylene pins was developed. Increase in the efficiency of 9-fluorenyl(methoxycarbonyl) N-terminal amino-protecting group removal was shown to have a greater influence on the accuracy of the “difficult” peptide synthesis than the use of more efficient amino acid coupling reagents such as aminium salts. Hence the unified schedule for multiple parallel solid-phase synthesis of “difficult” peptides included the procedure for N-terminal amino group deprotection modified by applying a more efficient reagent for the deprotection and the standard procedure of amino acid coupling by carbodiimide method with an additional coupling using aminium salts, if necessary. Amino acid coupling with the help of carbodiimide allows to follow the completeness of the coupling via the bromophenol blue indication, thus providing the accuracy of the synthesis and preventing an overexpenditure of expensive reagents. About 100 biotinylated hepatitis C virus envelope protein fragments, most of which represented “difficult” peptides, were successfully obtained by synthesis on pins with the help of the developed unified schedule.