| Literature DB >> 19213045 |
Lukasz Jaremko1, Mariusz Jaremko, Paweł Pasikowski, Marek Cebrat, Piotr Stefanowicz, Marek Lisowski, Jolanta Artym, Michał Zimecki, Igor Zhukov, Zbigniew Szewczuk.
Abstract
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. (c) 2009 Wiley Periodicals, Inc. Biopolymers 91: 423-431, 2009.Entities:
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Year: 2009 PMID: 19213045 DOI: 10.1002/bip.21160
Source DB: PubMed Journal: Biopolymers ISSN: 0006-3525 Impact factor: 2.505