Wydział Chemii

Monika Biernat

Marzena M. Cydzik

Piotr Stefanowicz

Alicja Kluczyk

Jolanta Artym

Michał Zimecki

Zbigniew Szewczuk

2016

Journal of Peptide Science

22

525-532

10.1002/psc.2898

Naukowa

Angielski

Artykuł

The nonapeptide fragment of the HLA-DR molecule, located in the exposed loop of the alpha-chain (164-172), having the VPRSGEVYT sequence, suppresses the immune response. Based on the three-dimensional structure of the HLA-DR superdimer, we designed a new cyclodimeric analog in which the two parallel peptide chains of VPRSGEVYT sequence are linked through their C-termini by spacer of (Gly5 )2 -Lys-NH2 and the N-termini are also linked by poly(ethylene glycol). The (VPRSGEVYTG5 )2 K-resin analog was synthesized using solid-phase peptide synthesis protocols. The cyclization was achieved by cross-linking the N-terminal positions of the dimeric peptide, attached to a MBHA resin, with alpha, omega-bis (acetic acid) poly(ethylene glycol), activated by esterification with pentafluorophenol. Our results demonstrate that the cyclodimerization of VPRSGEVYT results in enhanced immunosuppressive activity of the peptide. Mass spectrometry fragmentation analysis of the obtained cyclodimeric peptide is also presented.

ESI-MS/MS, HLA-DR analogs, PEG linker, cyclodimer

http://dx.doi.org/ 10.1002/psc.2898

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