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Evaluating the coupling efficiency of phosphorylated amino acids for SPOT synthesis
Author(s) -
Tapia Victor,
Ay Bernhard,
Triebus Julia,
Wolter Eike,
Boisguerin Prisca,
Volkmer Rudolf
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1068
Subject(s) - phosphopeptide , phosphorylation , threonine , serine , peptide , tyrosine , chemistry , amino acid , peptide synthesis , biochemistry , computational biology , protein phosphorylation , combinatorial chemistry , computer science , biology , protein kinase a
A high demand of interest concerning binding assays to study the consequences of posttranscriptional phosphorylation may be addressed by peptide array‐based methods. A crucial factor for de novo chemical approaches to generate such arrays is the possibility to rationally permutate phosphorylation events along a huge number of sequences. The simple principle behind this advantage is the stepwise synthesis of peptides, which allows the incorporation of either phosphorylated or nonphosphorylated derivates at serine, threonine, and tyrosine positions. In spite of several reported applications of phosphopeptide arrays, there is, to our best knowledge, no reported analysis of the efficiency of the involved techniques. Here, we analyze different coupling conditions to introduce phosphoamino acids in standard SPOT synthesis. Our results clearly indicate that EEDQ is the preferable activator and can also be used in fully automated SPOT synthesis. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.