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The immunosuppressive activity and solution structures of ubiquitin fragments
Author(s) -
Jaremko Łukasz,
Jaremko Mariusz,
Pasikowski Paweł,
Cebrat Marek,
Stefanowicz Piotr,
Lisowski Marek,
Artym Jolanta,
Zimecki Michał,
Zhukov Igor,
Szewczuk Zbigniew
Publication year - 2009
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21160
Subject(s) - chemistry , ubiquitin , peptide , preprint , deubiquitinating enzyme , sequence (biology) , biochemistry , computational biology , stereochemistry , biology , gene , world wide web , computer science
Recently, ubiquitin was suggested as a promising anti‐inflammatory protein therapeutic. We found that a peptide fragment corresponding to the ubiquitin 50–59 sequence (LEDGRTLSDY) possessed the immunosuppressive activity comparable with that of ubiquitin. CD and NMR spectroscopies were used to determine the conformational preferences of LEDGRTLSDY in solution. The peptide mixture, obtained by pepsin digestion of ubiquitin, was even more potent than the intact protein. Although the peptide exhibited a well‐defined conformation in methanol, its structure was distinct from the corresponding 50–59 fragment in the native ubiquitin molecule. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 423–431, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com