Repozytorium

The immunosuppressive activity and solution structures of ubiquitin fragments.

Autorzy

Łukasz Jaremko

Mariusz Jaremko

Paweł Pasikowski

Marek Cebrat

Piotr Stefanowicz

Marek Lisowski

Jolanta Artym

Michał Zimecki

Igor Zhukov

Zbigniew Szewczuk

Rok wydania

2009

Czasopismo

Biopolymers

Numer woluminu

91

Strony

423-431

DOI

10.1002/bip.21160

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

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.

Słowa kluczowe

ubiquitin, immunomodulation, retro‐RGD sequence, solution structure, NMR, peptic fragments, cryptides

Adres publiczny

https://doi.org/10.1002/bip.21160

Strona internetowa wydawcy

onlinelibrary.wiley.com

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