Proceedings book download - 5Z.com

The effect of dimeric analogs on the immunomodulatory activity was examined in the AFCin vitro experiment. The immunological tests show that N- and C-terminal dimerization didnot cause significant increase in the biological activity (compound 1 and compound 2). Incontrast, the increase in immunological activity in case of the parallel dimers (compound 3and compound 4) was observed. Compound 3, which contains a shorter linker, possesseshigher immunosuppressory potency than its analog 4 with a longer linker.Although mechanism of immunosuppressory action of ubiquitin fragments stillremains unknown, they may interrupt the interactions of ubiquitin with its hypotheticalreceptors. Since ubiquitin is known to exist in oligomeric form, a possibility of interactionof oligoubiquitin with some oligomeric receptors cannot be excluded.The enhanced immunosuppressory activity of the parallel dimers 3 and 4, as comparedto their anti-parallel analogs (compounds 1 and 2), may suggest a parallel orientation of themolecules of the hypothetic ubiquitin receptors responsible for the immunomodulatoryactivity.AcknowledgmentsThis work was supported in part by grant No. N N401 222734 from the Ministry of Science andHigher Education (Poland).References1. Szewczuk, Z., Biernat, M., Dyba, M., Zimecki, M. Peptides 25, 207-215 (2004).2. Biernat, M., Stefanowicz, P., Zimecki, M., Szewczuk, Z. Bioconjugate Chem. 17, 1116-1124 (2006).3. Pasikowski, P., Cydzik, M., Kluczyk, A., Stefanowicz, P., Szewczuk, Z. BioMol. Concepts 1, 67-83(2010).4. Szewczuk, Z., Stefanowicz, P., Wilczyński, A., Staszewska, A., Siemion, I.Z., Zimecki, M.,Wieczorek, Z. Biopolymers 74, 352-362 (2004).5. Jaremko, Ł., Jaremko, M., Pasikowski, P., Cebrat, M., Stefanowicz, P., Lisowski, M., Artym, J.,Zimecki, M., Zhukov, I., Szewczuk, Z. Biopolymers 91, 423-431 (2009).97