The immunosuppressive activity and solution structures of ubiquitin fragments

Łukasz Jaremko; Mariusz Jaremko; Paweł Pasikowski; Marek Cebrat; Piotr Stefanowicz; Marek Lisowski; Jolanta Artyin; Michał Zimecki; Igor Zhukov; Zbigniew Szewczuk

doi:10.1002/bip.21160

The immunosuppressive activity and solution structures of ubiquitin fragments

Łukasz Jaremko, Mariusz Jaremko, Paweł Pasikowski, Marek Cebrat, Piotr Stefanowicz, Marek Lisowski, Jolanta Artyin, Michał Zimecki, Igor Zhukov, Zbigniew Szewczuk

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

Recently, ubiquitin was suggested as a promising antiinflammatory 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.

Original language	English (US)
Pages (from-to)	423-431
Number of pages	9
Journal	Biopolymers
Volume	91
Issue number	6
DOIs	https://doi.org/10.1002/bip.21160
State	Published - 2009
Externally published	Yes

Keywords

Cryptides
Immunomodulation
NMR
Peptic fragments
Retro-RGD sequence
Solution structure
Ubiquitin

ASJC Scopus subject areas

Biochemistry
Biophysics
Biomaterials
Organic Chemistry

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10.1002/bip.21160

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abstract = "Recently, ubiquitin was suggested as a promising antiinflammatory protein therapeutic. We found that a peptide fragment corresponding to the ubiquitin50-59 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.",

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T1 - The immunosuppressive activity and solution structures of ubiquitin fragments

AU - Jaremko, Łukasz

AU - Jaremko, Mariusz

AU - Pasikowski, Paweł

AU - Cebrat, Marek

AU - Stefanowicz, Piotr

AU - Lisowski, Marek

AU - Artyin, Jolanta

AU - Zimecki, Michał

AU - Zhukov, Igor

AU - Szewczuk, Zbigniew

PY - 2009

Y1 - 2009

N2 - Recently, ubiquitin was suggested as a promising antiinflammatory protein therapeutic. We found that a peptide fragment corresponding to the ubiquitin50-59 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.

AB - Recently, ubiquitin was suggested as a promising antiinflammatory protein therapeutic. We found that a peptide fragment corresponding to the ubiquitin50-59 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.

KW - Cryptides

KW - Immunomodulation

KW - NMR

KW - Peptic fragments

KW - Retro-RGD sequence

KW - Solution structure

KW - Ubiquitin

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The immunosuppressive activity and solution structures of ubiquitin fragments

Abstract

Keywords

ASJC Scopus subject areas

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